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Information on EC 2.7.7.88 - GDP polyribonucleotidyltransferase
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EC Tree
2.7.7.88 GDP polyribonucleotidyltransferaseIUBMB Comments
The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA. cf. EC 2.7.7.50, mRNA guanylyltransferase.
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Word Map
- 2.7.7.88
- cap
-
unconventional
- vesicular
- stomatitis
- prntase
-
rna-dependent
- viruses
- measles
- ebola
-
nonsegmented
-
5'-monophosphorylated
-
negative-strand
- strand
- gpppa
- guanosine
- ppprna
-
phosphoamide
- 5'-diphosphate
-
guanylyltransferase
-
rhabdoviruses
- 5'-triphosphatase
- drug development
The enzyme appears in viruses and cellular organisms
Reaction Schemes
(5')pppAACA-[mRNA]
+
=
+
G(5')pppAACA-[mRNA]
Synonyms
gdp polyribonucleotidyltransferase, rna:gdp polyribonucleotidyltransferase, l-prna complex, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-triphospho-mRNA:GDP 5'-phosphopolyribonucleotidyltransferase [G(5')ppp-mRNA-forming]
-
-
-
-
5'-triphospho-mRNA:GDP5'-phosphopolyribonucleotidyltransferase
-
-
mRNA capping enzyme
non-segmented negative strand RNA viral mRNA capping enzyme
PRNTase
rabies virus large protein
RNA-directed RNA polymerase L
additional information
non-segmented negative strand RNA viral mRNA capping enzyme
-
non-segmented negative strand RNA viral mRNA capping enzyme
vesicular stomatitis Indiana virus Mudd-Summers
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5')pppAACA-[mRNA] + GDP = diphosphate + G(5')pppAACA-[mRNA]
(overall reaction)
-
-
-
(5')pppAACA-[mRNA] + [protein L]-L-histidine = diphosphate + [protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + H2O
(1a)
-
-
-
[protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + GDP + H2O = [protein L]-L-histidine + G(5')pppAACA-[mRNA]
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(5')pppAACA-[mRNA]:GDP 5'-phosphopolyribonucleotidyltransferase [(5')pppAACA-[mRNA]-forming]
The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA. cf. EC 2.7.7.50, mRNA guanylyltransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-triphospho-AACAG + 2,6-diaminopurine-riboside 5'-diphosphate
diphosphate + 2,6-diaminopurine-riboside 5'-triphospho-AACAG
-
-
-
-
?
5'-triphospho-AACAG + 7-deazaguanosine 5'-diphosphate
diphosphate + 7-deazaguanosine 5'-triphospho-AACAG
-
-
-
-
?
5'-triphospho-AACAG + 7-methylguanosine 5'-diphosphate
diphosphate + 7-methylguanosine 5'-triphospho-AACAG
-
-
-
-
?
5'-triphospho-AACAG + GDP
diphosphate + guanosine 5'-triphospho-AACAG
-
-
-
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
pppAACAG + GDP
diphosphate + guanosine 5'-pppAACAG
-
oligo-RNa substrate. Residues G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E are essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies Pasteur vaccins
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies PV
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
vesicular stomatitis Indiana virus Mudd-Summers
overall reaction
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
Lyssavirus rabies
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
Lyssavirus rabies Nishigahara RCEH
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
enzyme produces a 5'-cap core structure, guanosine(5')triphospho(5')adenosine (GpppA), on viral mRNA
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
enzyme produces a 5'-cap core structure, guanosine(5')triphospho(5')adenosine (GpppA), on viral mRNA
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
the enzyme specifically reacts with a viral mRNA start-sequence (5'-AACAG) with a 5'-triphosphate group
-
-
?
5'-triphospho-mRNA + GTP
diphosphate + guanosine 5'-tetraphospho-mRNA
-
additional reaction, the unusual cap structure guanosine(5')tetraphospho(5')adenosine (GppppA) is formed by the transfer of the 5'-monophosphorylated viral mRNA start sequence to GTP by the PRNTase activity before the removal of the gamma-phosphate from GTP by GTPase. GppppA-capped and polyadenylated full-length mRNAs are also synthesized by an in vitro transcription system
-
?
5'-triphospho-mRNA + GTP
diphosphate + guanosine 5'-tetraphospho-mRNA
-
additional reaction, the unusual cap structure guanosine(5')tetraphospho(5')adenosine (GppppA) is formed by the transfer of the 5'-monophosphorylated viral mRNA start sequence to GTP by the PRNTase activity before the removal of the gamma-phosphate from GTP by GTPase. GppppA-capped and polyadenylated full-length mRNAs are also synthesized by an in vitro transcription system
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
Lyssavirus rabies
overall reaction
-
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
Lyssavirus rabies Pasteur vaccins
overall reaction
-
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
Lyssavirus rabies PV
overall reaction
-
-
?
pppApApCpApG + GDP
diphosphate + guanosine 5'-pppApApCpApG
-
recombinant enzyme specifically caps pppApApCpApG with GDP
-
?
pppApApCpApG + GDP
diphosphate + guanosine 5'-pppApApCpApG
-
recombinant enzyme specifically caps pppApApCpApG with GDP
-
?
additional information
?
-
Lyssavirus rabies
rabies virus large structural protein shows guanosine 51-triphosphatase and GDP polyribonucleotidyltransferase activities. Enzyme caps 5'-triphosphorylated but not 5'-diphosphorylated RABV mRNA-start sequences, 5'-AACA(C/U), with GDP to generate the 5'-terminal cap structure G(5')ppp(5')A. The 5'-AAC sequence in the substrate RNAs is strictly essential for RNA capping with the RABV L protein
-
-
?
additional information
?
-
Lyssavirus rabies
structure-function analysis, and substrate binding structure analysis, overview
-
-
-
additional information
?
-
Lyssavirus rabies Nishigahara RCEH
rabies virus large structural protein shows guanosine 51-triphosphatase and GDP polyribonucleotidyltransferase activities. Enzyme caps 5'-triphosphorylated but not 5'-diphosphorylated RABV mRNA-start sequences, 5'-AACA(C/U), with GDP to generate the 5'-terminal cap structure G(5')ppp(5')A. The 5'-AAC sequence in the substrate RNAs is strictly essential for RNA capping with the RABV L protein
-
-
?
additional information
?
-
Lyssavirus rabies Pasteur vaccins
structure-function analysis, and substrate binding structure analysis, overview
-
-
-
additional information
?
-
Lyssavirus rabies PV
structure-function analysis, and substrate binding structure analysis, overview
-
-
-
additional information
?
-
a 5'-monophosphorylated viral mRNA-start sequence is transferred to GDP generated from GTP via a covalent enzyme-RNA intermediate. The enzyme uses only 5'-triphosphorylated RNA substrates. It efficiently caps RNAs containing an A(purine)CNG sequence with GDP. Especially, the first A and third pyrimidine residues appear to be essential for the RNA substrate activity. No substrates: ppApApCpApG or pppApCpGpApA
-
-
?
additional information
?
-
GppppA is efficiently formed on RNAs containing the ARCNG sequence. When GACAG RNA is used, no possible cap structures, such as GpppG and GppppG, are formed. AAGAG and ACGAA RNAs are obviously inert as substrates for GpppA formation with GTP as well as GDP
-
-
?
additional information
?
-
sequence-specific recognition of mRNA 5'-ends with the VSV PRNTase domain. The enzyme assay is performed with recombinant wild-type or mutant VSV L protein using [alpha-32P]GDP and pppAACAG oligo-RNA as substrates
-
-
-
additional information
?
-
vesicular stomatitis Indiana virus Mudd-Summers
sequence-specific recognition of mRNA 5'-ends with the VSV PRNTase domain. The enzyme assay is performed with recombinant wild-type or mutant VSV L protein using [alpha-32P]GDP and pppAACAG oligo-RNA as substrates
-
-
-
additional information
?
-
GppppA is efficiently formed on RNAs containing the ARCNG sequence. When GACAG RNA is used, no possible cap structures, such as GpppG and GppppG, are formed. AAGAG and ACGAA RNAs are obviously inert as substrates for GpppA formation with GTP as well as GDP
-
-
?
additional information
?
-
a 5'-monophosphorylated viral mRNA-start sequence is transferred to GDP generated from GTP via a covalent enzyme-RNA intermediate. The enzyme uses only 5'-triphosphorylated RNA substrates. It efficiently caps RNAs containing an A(purine)CNG sequence with GDP. Especially, the first A and third pyrimidine residues appear to be essential for the RNA substrate activity. No substrates: ppApApCpApG or pppApCpGpApA
-
-
?
additional information
?
-
-
free 5'-phosphorylated mRNA is completely inert as a substrate
-
-
?
additional information
?
-
-
the enzyme is capable of transferring a polyribonucleotidyl group to a substrate using a catalytic histidine residue. The histidine-arginine motif is required for the enzyme activity at the step of the enzyme-5'-phosphorylated mRNA intermediate formation
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies Pasteur vaccins
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
Lyssavirus rabies PV
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
overall reaction
-
-
?
(5')pppAACA-[mRNA] + GDP
diphosphate + G(5')pppAACA-[mRNA]
vesicular stomatitis Indiana virus Mudd-Summers
overall reaction
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
-
-
-
?
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
-
the enzyme specifically reacts with a viral mRNA start-sequence (5'-AACAG) with a 5'-triphosphate group
-
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
Lyssavirus rabies
overall reaction
-
-
?
a 5'-end triphospho-adenylyl-adenylyl-cytidyl-adenosine in mRNA + GDP + H+
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidyl-adenosine in mRNA + diphosphate
Lyssavirus rabies Pasteur vaccins
overall reaction
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
assay in presence of 1 mM divalent cation, Mn2+ is preferred over Mg2+
Mg2+
assay in presence of 1 mM divalent cation, Mn2+ is preferred over Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphate
inhibits formation of the enzyme-RNa complex
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Rabies
5'-Phospho-RNA Acceptor Specificity of GDP Polyribonucleotidyltransferase of Vesicular Stomatitis Virus in mRNA Capping.
Rabies
The Rabies Virus L Protein Catalyzes mRNA Capping with GDP Polyribonucleotidyltransferase Activity.
Rabies
Transcriptional Control and mRNA Capping by the GDP Polyribonucleotidyltransferase Domain of the Rabies Virus Large Protein.
Vesicular Stomatitis
5'-Phospho-RNA Acceptor Specificity of GDP Polyribonucleotidyltransferase of Vesicular Stomatitis Virus in mRNA Capping.
Vesicular Stomatitis
Formation of guanosine(5')tetraphospho(5')adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus.
Vesicular Stomatitis
Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00038
2',3'-dideoxyguanosine 5'-diphosphate
-
at pH 7.5 and 30°C
0.000036
2,6-diaminopurine-riboside 5'-diphosphate
-
at pH 7.5 and 30°C
0.00014
2-aminopurine-riboside 5'-diphosphate
-
at pH 7.5 and 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
2,6-diaminopurine-riboside 5'-diphosphate
vesicular stomatitis virus
-
at pH 7.5 and 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Lyssavirus rabies
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Lyssavirus rabies
the putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids) with those in L proteins of NNS RNA viruses belonging to the the order Mononegavirales. The structural model of the putative RABV PRNTase domain suggests that it possesses a large loop structure flanking the PRNTase motif B, which corresponds to a priming loop proposed for the VSV L protein
evolution
the unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) or block V domain in RNA polymerase L proteins of nonsegmented negative strand (NNS) RNA viruses (e.g. rabies, measles, Ebola) contains five collinear sequence elements, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Identification of conserved motifs in putative PRNTase domains. Phylogenetic analysis of putative PRNTase domains in NNS RNA viral L proteins, overview
evolution
Lyssavirus rabies PV
-
the putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids) with those in L proteins of NNS RNA viruses belonging to the the order Mononegavirales. The structural model of the putative RABV PRNTase domain suggests that it possesses a large loop structure flanking the PRNTase motif B, which corresponds to a priming loop proposed for the VSV L protein
-
evolution
Lyssavirus rabies Pasteur vaccins
-
the putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids) with those in L proteins of NNS RNA viruses belonging to the the order Mononegavirales. The structural model of the putative RABV PRNTase domain suggests that it possesses a large loop structure flanking the PRNTase motif B, which corresponds to a priming loop proposed for the VSV L protein
-
evolution
vesicular stomatitis Indiana virus Mudd-Summers
-
the unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) or block V domain in RNA polymerase L proteins of nonsegmented negative strand (NNS) RNA viruses (e.g. rabies, measles, Ebola) contains five collinear sequence elements, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Identification of conserved motifs in putative PRNTase domains. Phylogenetic analysis of putative PRNTase domains in NNS RNA viral L proteins, overview
-
malfunction
Cap-defective mutants produce uncapped abortive transcripts by aberrant stop-start transcription. Cap defective mutations in these residues induced termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolished virus gene expression in host cells
malfunction
vesicular stomatitis Indiana virus Mudd-Summers
-
Cap-defective mutants produce uncapped abortive transcripts by aberrant stop-start transcription. Cap defective mutations in these residues induced termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolished virus gene expression in host cells
-
metabolism
Lyssavirus rabies
molecular mechanisms of RABV RNA biogenesis, overview. In the second step, the PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA. Roles of RABV replication proteins in transcription and replication, and unique RABV machineries required for mRNA capping and transcription initiation. Comparison of Rabies virus mechanism of mRNA capping with that of eukaryotic cells
metabolism
Lyssavirus rabies PV
-
molecular mechanisms of RABV RNA biogenesis, overview. In the second step, the PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA. Roles of RABV replication proteins in transcription and replication, and unique RABV machineries required for mRNA capping and transcription initiation. Comparison of Rabies virus mechanism of mRNA capping with that of eukaryotic cells
-
metabolism
Lyssavirus rabies Pasteur vaccins
-
molecular mechanisms of RABV RNA biogenesis, overview. In the second step, the PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA. Roles of RABV replication proteins in transcription and replication, and unique RABV machineries required for mRNA capping and transcription initiation. Comparison of Rabies virus mechanism of mRNA capping with that of eukaryotic cells
-
physiological function
RNA polymerase L protein shows RNA:GDP polyribonucleotidyltransferase activity, which transfers the 5'-monophosphorylated viral mRNA start sequence to GDP to produce a capped RNA. The conserved HR motif in the L protein is essential for the this activity. L protein forms two distinct SDS-resistant complexes with the mRNA and leader RNA start sequences, mutations in the HR motif significantly reduce the formation of the former complex, but not the latter complex
physiological function
the conserved motifs constitute the active site of the PRNTase domain and the L-pRNA intermediate formation followed by the cap formation is essential for successful synthesis of full-length mRNAs. The PRNTase motifs are required for VSV gene expression in host cells
physiological function
Lyssavirus rabies
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase. Transcriptional control and mRNA capping are exerted by the GDP polyribonucleotidyltransferase domain of the rabies virus large protein. It catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. The PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA, roles of the GDP polyribonucleotidyltransferase (PRNTase) domain of the rabies virus (RABV) large (L) protein in transcription initiation and pre-mRNA capping
physiological function
Lyssavirus rabies PV
-
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase. Transcriptional control and mRNA capping are exerted by the GDP polyribonucleotidyltransferase domain of the rabies virus large protein. It catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. The PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA, roles of the GDP polyribonucleotidyltransferase (PRNTase) domain of the rabies virus (RABV) large (L) protein in transcription initiation and pre-mRNA capping
-
physiological function
Lyssavirus rabies Pasteur vaccins
-
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase. Transcriptional control and mRNA capping are exerted by the GDP polyribonucleotidyltransferase domain of the rabies virus large protein. It catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. The PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA, roles of the GDP polyribonucleotidyltransferase (PRNTase) domain of the rabies virus (RABV) large (L) protein in transcription initiation and pre-mRNA capping
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physiological function
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RNA polymerase L protein shows RNA:GDP polyribonucleotidyltransferase activity, which transfers the 5'-monophosphorylated viral mRNA start sequence to GDP to produce a capped RNA. The conserved HR motif in the L protein is essential for the this activity. L protein forms two distinct SDS-resistant complexes with the mRNA and leader RNA start sequences, mutations in the HR motif significantly reduce the formation of the former complex, but not the latter complex
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physiological function
vesicular stomatitis Indiana virus Mudd-Summers
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the conserved motifs constitute the active site of the PRNTase domain and the L-pRNA intermediate formation followed by the cap formation is essential for successful synthesis of full-length mRNAs. The PRNTase motifs are required for VSV gene expression in host cells
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additional information
Lyssavirus rabies
residues G1112 in motif A, T1170 in motif B, W1201 in motif C, H1241 and R1242 in motif D, and F1285 and Q1286 in motif E are identified as essential for the PRNTase activity of the RABV L protein. The RABV counterpart (H1241) of the VSV H1227 residue can be predicted to serve as a covalent pRNA attachment site for the putative L-pRNA intermediate formation. Structure and structure-function analysis, overview
additional information
signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation, overview. Similar to the catalytic residues in motif D, G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E were found to be essential or important for the PRNTase activity in the step of the covalent LpRNA intermediate formation, but not for the GTPase activity that generates GDP (pRNA acceptor)
additional information
Lyssavirus rabies PV
-
residues G1112 in motif A, T1170 in motif B, W1201 in motif C, H1241 and R1242 in motif D, and F1285 and Q1286 in motif E are identified as essential for the PRNTase activity of the RABV L protein. The RABV counterpart (H1241) of the VSV H1227 residue can be predicted to serve as a covalent pRNA attachment site for the putative L-pRNA intermediate formation. Structure and structure-function analysis, overview
-
additional information
Lyssavirus rabies Pasteur vaccins
-
residues G1112 in motif A, T1170 in motif B, W1201 in motif C, H1241 and R1242 in motif D, and F1285 and Q1286 in motif E are identified as essential for the PRNTase activity of the RABV L protein. The RABV counterpart (H1241) of the VSV H1227 residue can be predicted to serve as a covalent pRNA attachment site for the putative L-pRNA intermediate formation. Structure and structure-function analysis, overview
-
additional information
vesicular stomatitis Indiana virus Mudd-Summers
-
signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation, overview. Similar to the catalytic residues in motif D, G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E were found to be essential or important for the PRNTase activity in the step of the covalent LpRNA intermediate formation, but not for the GTPase activity that generates GDP (pRNA acceptor)
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Show AA Sequence and Transmembrane Helices (8106 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Lyssavirus rabies
the RABV L protein is predicted to have an N-terminal (NTD, composed of subdomains I and II), RdRp, bridge, mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase), connector (CD), methyltransferase (MTase), and C-terminal (CTD) domains, model of the rabies virus (RABV) large (L) protein, and domain organization, three-dimensional structure of the RABV L protein, overview. The putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Structure analysis, overview
additional information
Lyssavirus rabies Pasteur vaccins
-
the RABV L protein is predicted to have an N-terminal (NTD, composed of subdomains I and II), RdRp, bridge, mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase), connector (CD), methyltransferase (MTase), and C-terminal (CTD) domains, model of the rabies virus (RABV) large (L) protein, and domain organization, three-dimensional structure of the RABV L protein, overview. The putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Structure analysis, overview
-
additional information
Lyssavirus rabies PV
-
the RABV L protein is predicted to have an N-terminal (NTD, composed of subdomains I and II), RdRp, bridge, mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase), connector (CD), methyltransferase (MTase), and C-terminal (CTD) domains, model of the rabies virus (RABV) large (L) protein, and domain organization, three-dimensional structure of the RABV L protein, overview. The putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Structure analysis, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G1112A
Lyssavirus rabies Nishigahara RCEH
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mutation abolishes RNA capping activity
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H1241A
Lyssavirus rabies Nishigahara RCEH
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mutation abolishes RNA capping activity
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R1242A
Lyssavirus rabies Nishigahara RCEH
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mutation abolishes RNA capping activity
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T1170A
Lyssavirus rabies Nishigahara RCEH
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mutation abolishes RNA capping activity
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W1201A
Lyssavirus rabies Nishigahara RCEH
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mutation abolishes RNA capping activity
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F1269W
site-directed mutagenesis, plaque phenotype compared to wild-type enzyme, the mutant shows 18% activity compared to wild-type
F1269Y
site-directed mutagenesis, plaque phenotype compared to wild-type enzyme, the mutant shows 31% activity compared to wild-type
G1100A
site-directed mutagenesis, the mutant shows 11% activity compared to wild-type
K1156A
site-directed mutagenesis, the mutant shows 81% activity compared to wild-type
L1153A
site-directed mutagenesis, the mutant shows 10% activity compared to wild-type
L1153F
site-directed mutagenesis, the mutant shows 3% activity compared to wild-type
L1153I
site-directed mutagenesis, the mutant shows 45% activity compared to wild-type
L1153V
site-directed mutagenesis, the mutant shows 39% activity compared to wild-type
P1104A
site-directed mutagenesis, the mutant shows 12% activity compared to wild-type
P1104V
site-directed mutagenesis, the mutant shows 15% activity compared to wild-type
S1155A
site-directed mutagenesis, the mutant shows 20% activity compared to wild-type
S1155G
site-directed mutagenesis, the mutant shows 53% activity compared to wild-type
S1155T
site-directed mutagenesis, the mutant shows 44% activity compared to wild-type
S1155V
site-directed mutagenesis, the mutant shows 2% activity compared to wild-type
S1158A
site-directed mutagenesis, the mutant shows 88% activity compared to wild-type
W1094A
site-directed mutagenesis, the mutant shows 136% activity compared to wild-type
W1094F
site-directed mutagenesis, the mutant shows 181% activity compared to wild-type
Y1152F
site-directed mutagenesis, the mutant shows 4% activity compared to wild-type
G1100A
vesicular stomatitis Indiana virus Mudd-Summers
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site-directed mutagenesis, the mutant shows 11% activity compared to wild-type
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P1104A
vesicular stomatitis Indiana virus Mudd-Summers
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site-directed mutagenesis, the mutant shows 12% activity compared to wild-type
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P1104V
vesicular stomatitis Indiana virus Mudd-Summers
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site-directed mutagenesis, the mutant shows 15% activity compared to wild-type
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S1155A
vesicular stomatitis Indiana virus Mudd-Summers
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site-directed mutagenesis, the mutant shows 20% activity compared to wild-type
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Y1152A
vesicular stomatitis Indiana virus Mudd-Summers
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site-directed mutagenesis, inactive mutant
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F1269A
F1269W
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the mutant shows 18% activity compared to the wild type enzyme
F1269Y
-
the mutant shows 31% activity compared to the wild type enzyme
G1100A
G1154A
K1156A
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the mutant shows 81% activity compared to the wild type enzyme
L1153A
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the mutant shows 10% activity compared to the wild type enzyme
L1153F
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the mutant shows 3% activity compared to the wild type enzyme
L1153I
-
the mutant shows 45% activity compared to the wild type enzyme
L1153V
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the mutant shows 39% activity compared to the wild type enzyme
P1104A
P1104V
Q1270A
S1155A
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the mutant shows 20% activity compared to the wild type enzyme
S1155G
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the mutant shows 53% activity compared to the wild type enzyme
S1155T
-
the mutant shows 44% activity compared to the wild type enzyme
S1155V
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the mutant shows 2% activity compared to the wild type enzyme
S1158A
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the mutant shows 88% activity compared to the wild type enzyme
T1157A
T1157S
W1094A
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the mutant shows 136% activity compared to the wild type enzyme
W1094F
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the mutant shows 181% activity compared to the wild type enzyme
W1188A
Y1152A
Y1152F
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the mutant shows 4% activity compared to the wild type enzyme
Y1152W
F1269A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
G1100A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
G1100A
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the mutant shows 11% activity compared to the wild type enzyme
G1154A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
P1104A
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the mutant shows 12% activity compared to the wild type enzyme
P1104A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
P1104V
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the mutant shows 15% activity compared to the wild type enzyme
P1104V
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Q1270A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
T1157A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
T1157S
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
W1188A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Y1152A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Y1152W
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from insect cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene L, genomic structure, transcription and replication of the rabies virus (RABV) genome. The negative-strand RABV genome wrapped with the nucleocapsid (N) proteins serves as a template for transcription and replication. The RNA-dependent RNA polymerase (RdRp, the complex between large (L) and (P) phosphoproteins) sequentially transcribes the leader region (Le) and five internal genes (N, P, M, G, and L) in the genome into the leader RNA (LeRNA) and five monocistronic mRNAs with the 5'-cap 1 and 3'-poly(A) structures by the stop-start transcription mechanism
Lyssavirus rabies
gene L, phylogenetic analysis, functional recombinant expression of wild-type and mutant enzymes in insect cells. The PRNTase motifs are required for VSV gene expression in host cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
Lyssavirus rabies
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase, which is one of the most attractive targets for developing antiviral agents
drug development
Lyssavirus rabies PV
-
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase, which is one of the most attractive targets for developing antiviral agents
-
drug development
Lyssavirus rabies Pasteur vaccins
-
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase, which is one of the most attractive targets for developing antiviral agents
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogino, T.; Banerjee, A.K.
The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity
J. Gen. Virol.
91
1311-1314
2010
Chandipura virus (P13179), Chandipura virus, Chandipura virus I653514 (P13179)
brenda
Ogino, T.; Banerjee, A.K.
Formation of guanosine(5)tetraphospho(5)adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus
J. Virol.
82
7729-7734
2008
vesicular stomatitis Indiana virus (P03523), vesicular stomatitis Indiana virus San Juan (P03523)
brenda
Ogino, T.; Banerjee, A.K.
Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus
Mol. Cell
25
85-97
2007
vesicular stomatitis Indiana virus (P03523), vesicular stomatitis Indiana virus San Juan (P03523)
brenda
Neubauer, J.; Ogino, M.; Green, T.J.; Ogino, T.
Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation
Nucleic Acids Res.
44
330-341
2016
vesicular stomatitis virus
brenda
Ogino, M.; Ito, N.; Sugiyama, M.; Ogino, T.
The rabies virus L protein catalyzes mRNA capping with GDP polyribonucleotidyltransferase activity
Viruses
8
144
2016
Lyssavirus rabies (Q9IPJ5), Lyssavirus rabies Nishigahara RCEH (Q9IPJ5)
brenda
Ogino, M.; Ogino, T.
5'-Phospho-RNA acceptor specificity of GDP polyribonucleotidyltransferase of vesicular stomatitis virus in mRNA capping
J. Virol.
91
e02322-16
2017
vesicular stomatitis virus
brenda
Ogino, T.; Yadav, S.P.; Banerjee, A.K.
Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase
Proc. Natl. Acad. Sci. USA
107
3463-3468
2010
vesicular stomatitis virus
brenda
Neubauer, J.; Ogino, M.; Green, T.; Ogino, T.
Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation
Nucleic Acids Res.
44
330-341
2016
vesicular stomatitis virus, vesicular stomatitis Indiana virus (Q98776), vesicular stomatitis Indiana virus Mudd-Summers (Q98776)
brenda
Ogino, T.; Green, T.J.
Transcriptional control and mRNA capping by the GDP polyribonucleotidyltransferase domain of the rabies virus large protein
Viruses
11
504
2019
Lyssavirus rabies (P11213), Lyssavirus rabies PV (P11213), Lyssavirus rabies Pasteur vaccins (P11213)
brenda
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