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S-adenosyl-L-methionine + pseudouridine in 5'-GAUPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-GAUmethylPsiCAACGCC-3'
S-adenosyl-L-methionine + pseudouridine in 5'-PsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-methylPsiCAACGCC-3'
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGC--3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGC--3'
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGCC-3'
S-adenosyl-L-methionine + pseudouridine54 in elongator tRNAMet
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in elongator tRNAMet
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
S-adenosyl-L-methionine + pseudouridine54 in tRNATrp
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNATrp
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additional information
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S-adenosyl-L-methionine + pseudouridine in 5'-GAUPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-GAUmethylPsiCAACGCC-3'
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S-adenosyl-L-methionine + pseudouridine in 5'-GAUPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-GAUmethylPsiCAACGCC-3'
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S-adenosyl-L-methionine + pseudouridine in 5'-PsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-methylPsiCAACGCC-3'
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?
S-adenosyl-L-methionine + pseudouridine in 5'-PsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-methylPsiCAACGCC-3'
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S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGC--3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGC--3'
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S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGC--3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGC--3'
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?
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGCC-3'
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?
S-adenosyl-L-methionine + pseudouridine in 5'-UPsiCAACGCC-3'
S-adenosyl-L-homocysteine + N1-methylpseudouridine in 5'-UmethylPsiCAACGCC-3'
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
methylation of pseudouridine PSI at position 54 of tRNA, producing m1PSI, in vitro pseudouridylated tRNATrp is used as a substrate
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
methylation of pseudouridine PSI at position 54 of tRNA, producing m1PSI, in vitro pseudouridylated tRNATrp is used as a substrate
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
methylation of pseudouridine PSI at position 54 of tRNA, producing m1PSI, in vitro pseudouridylated tRNATrp is used as a substrate
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
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S-adenosyl-L-methionine + pseudouridine54 in tRNA
S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
methylation of pseudouridine PSI at position 54 of tRNA, in vitro and in vivo reaction, producing m1PSI, in vitro pseudouridylated tRNATrp is used as a substrate
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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enzymatic post-transcriptional modifications of selected uridines in tRNA, secondary structure, U54 targets within the highly conserved 7-nt TPSI-loop, overview
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additional information
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Mja_1640 methylates T-arm resembling tRNAs in vitro. Using synthetic 17 mer RNAs resembling the T-arm of Methanocaldococcus jannaschii tRNATrp that contains a pseudouridine at either position 54, 55, or both, the capability of MjNep1 to methylate these substrates is shown, MjNep1 methylates the substrate with a pseudouridine at position 55 with reasonable efficiency, but markedly slower than its native small ribosomal subunit rRNA-derived substrate, and no methylation is observed for the substrate with pseudouridine at position 54, MjNep1 is incapable of modifying mature H. volcanii tRNAs. MjNep1 is apparently not the pseudouridine-N1 methyltransferase responsible for the tRNA-modification at position 54 in archaeal tRNAs
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additional information
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Mja_1640 methylates T-arm resembling tRNAs in vitro. Using synthetic 17 mer RNAs resembling the T-arm of Methanocaldococcus jannaschii tRNATrp that contains a pseudouridine at either position 54, 55, or both, the capability of MjNep1 to methylate these substrates is shown, MjNep1 methylates the substrate with a pseudouridine at position 55 with reasonable efficiency, but markedly slower than its native small ribosomal subunit rRNA-derived substrate, and no methylation is observed for the substrate with pseudouridine at position 54, MjNep1 is incapable of modifying mature H. volcanii tRNAs. MjNep1 is apparently not the pseudouridine-N1 methyltransferase responsible for the tRNA-modification at position 54 in archaeal tRNAs
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additional information
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SAM-binding pocket Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation, RNA-binding residues and putative active site, overview
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additional information
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SAM-binding pocket Asp157 or Glu183 from its own monomer or Ser43 from the associate monomer probably plays the catalytic role for RNA methylation, RNA-binding residues and putative active site, overview
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additional information
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substrate specificity analysis by NMR binding and affinity study for RNA, overview. The enzyme is highly specific for pseudouridine. Methanocaldococcus jannaschii Nep1 binds to the yeast Nep1 RNA consensus sequence
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additional information
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substrate specificity analysis by NMR binding and affinity study for RNA, overview. The enzyme is highly specific for pseudouridine. Methanocaldococcus jannaschii Nep1 binds to the yeast Nep1 RNA consensus sequence
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additional information
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substrate specificity analysis by NMR binding and affinity study for RNA, overview. The enzyme is highly specific for pseudouridine. Methanocaldococcus jannaschii Nep1 binds to the yeast Nep1 RNA consensus sequence
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evolution
m1PSI formation in archaeal tRNAs, overview. The enzyme belongs to Cluster of Orthologous Group, COG, 1901
evolution
m1PSI formation in archaeal tRNAs, overview. The enzyme belongs to Cluster of Orthologous Group, COG, 1901
evolution
m1PSI formation in archaeal tRNAs, overview. The enzyme belongs to Cluster of Orthologous Group, COG, 1901
evolution
Nep1 structure reveals a dimer with a fold similar to the SPOUT-class of RNA-methyltransferases
evolution
Nep1 structure reveals a dimer with a fold similar to the SPOUT-class of RNA-methyltransferases
evolution
phylogeny of the methyltransferase family, overview
evolution
the enzyme is a member of the SPOUT-class family of RNA methyltransferases, phylogeny of the methyltransferase family, overview
evolution
the enzyme is a SPOUT-class RNA methyltransferase and belongs to the DUF358 family. The DUF358/Mj1640 protein shows close structural relationship to Nep1, a pseudouridine-N1-specific rRNA methyltransferase
evolution
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Nep1 structure reveals a dimer with a fold similar to the SPOUT-class of RNA-methyltransferases
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evolution
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m1PSI formation in archaeal tRNAs, overview. The enzyme belongs to Cluster of Orthologous Group, COG, 1901
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malfunction
a Hvo_1989 knockout strain lacks N1-methyl pseudouridine modifications at position 54 of its tRNAs, the in-frame deletion of the pseudouridine N1-methyltransferase gene in Haloferax volcanii does not result in a discernable phenotype
malfunction
a mutation in the human Nep1 homolog causes Bowen-Conradi syndrome, a severe developmental disorder
malfunction
deletion of trmY leads to the absence of m1PSI54 in Haloferax volcanii tRNA
metabolism
Pus10-mediated PSI54 (and PSI55) formation does not require the presence of TrmY activity, overview
metabolism
Pus10-mediated PSI54 (and PSI55) formation does not require the presence of TrmY activity, overview
physiological function
Nep1 acts as a methyltransferase in ribosome biogenesis
physiological function
Nep1 acts as a methyltransferase in ribosome biogenesis
physiological function
trmY is not essential in Haloferax volcanii
physiological function
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Nep1 acts as a methyltransferase in ribosome biogenesis
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additional information
Methanocaldococcus jannaschii TrmY requires C55 (or possibly U55) in the tRNA to produce m1PSI54
additional information
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Methanocaldococcus jannaschii TrmY requires C55 (or possibly U55) in the tRNA to produce m1PSI54
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Chen, H.; Yuan, Y.
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase
J. Mol. Cell Biol.
2
366-374
2010
Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii
brenda
Wurm, J.; Meyer, B.; Bahr, U.; Held, M.; Frolow, O.; Koetter, P.; Engels, J.; Heckel, A.; Karas, M.; Entian, K.; Woehnert, J.
The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase
Nucleic Acids Res.
38
2387-2398
2010
Methanocaldococcus jannaschii (Q57977), Methanocaldococcus jannaschii, Homo sapiens (Q92979), Homo sapiens, Methanocaldococcus jannaschii DSM 2661 (Q57977)
brenda
Wurm, J.; Griese, M.; Bahr, U.; Held, M.; Heckel, A.; Karas, M.; Soppa, J.; Woehnert, J.
Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs
RNA
18
412-420
2012
Haloferax volcanii (D4GTL8), Haloferax volcanii, Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii
brenda
Chatterjee, K.; Blaby, I.K.; Thiaville, P.C.; Majumder, M.; Grosjean, H.; Yuan, Y.A.; Gupta, R.; de Crecy-Lagard, V.
The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA
RNA
18
421-433
2012
Haloferax volcanii (D4GTL8), Haloferax volcanii, Methanocaldococcus jannaschii (Q59034), Methanocaldococcus jannaschii, Halobacterium sp. (Q9HNR6), Halobacterium sp., Halobacterium sp. NRC-1 (Q9HNR6)
brenda