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L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
additional information
?
-
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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i.e. G+, which is found only in Archaea at position 15 in the dihydrouridine loop, i.e. D-loop
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?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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i.e. preQ0-tRNA
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L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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preQ0-tRNASer is used as substrate
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?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
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?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
preQ0-tRNASer is used as substrate
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
preQ0-tRNASer is used as substrate
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
preQ0-tRNASer is used as substrate
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha. G+ is successfully synthesized in recombinant Escherichia coli cells by MaArcTGT and the MaArcS-MaRaSEA complex
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha. G+ is successfully synthesized in recombinant Escherichia coli cells by MaArcTGT and the MaArcS-MaRaSEA complex
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha. G+ is successfully synthesized in recombinant Escherichia coli cells by MaArcTGT and the MaArcS-MaRaSEA complex
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha. G+ is successfully synthesized in recombinant Escherichia coli cells by MaArcTGT and the MaArcS-MaRaSEA complex
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
i.e. G+, whcih is found only in Archaea at position 15 in the dihydrouridine loop, i.e. D-loop
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
i.e. preQ0-tRNA
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
-
?
additional information
?
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recombinant MjTgtA2 converts preQ0-tRNA to G+-tRNA using several nitrogen sources and to do so in an ATP-independent process. MjTgtA2 shows in vitro glutaminase activity
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?
additional information
?
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recombinant MjTgtA2 converts preQ0-tRNA to G+-tRNA using several nitrogen sources and to do so in an ATP-independent process. MjTgtA2 shows in vitro glutaminase activity
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?
additional information
?
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recombinant MjTgtA2 converts preQ0-tRNA to G+-tRNA using several nitrogen sources and to do so in an ATP-independent process. MjTgtA2 shows in vitro glutaminase activity
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-
?
additional information
?
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in the Escherichia coli K12 MG1655 strain, the queF and queC are deleted (DELTAque/DELTAqueF), and the resulting deletion strain is transformed with an expression plasmid containing GAT-queC from Ssulfolobus solfataricus (SSO0016) cloned behind a PBAD promoter. Peaks corresponding to 7-amidino-7-deazaguanosine (archaeosine) and 7-cyano-7-deazaguanine nucleoside are detected in tRNA extracted from the strain expressing SSO0016
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?
additional information
?
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in the Escherichia coli K12 MG1655 strain, the queF and queC are deleted (DELTAque/DELTAqueF), and the resulting deletion strain is transformed with an expression plasmid containing GAT-queC from Ssulfolobus solfataricus (SSO0016) cloned behind a PBAD promoter. Peaks corresponding to 7-amidino-7-deazaguanosine (archaeosine) and 7-cyano-7-deazaguanine nucleoside are detected in tRNA extracted from the strain expressing SSO0016
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
i.e. G+, which is found only in Archaea at position 15 in the dihydrouridine loop, i.e. D-loop
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
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-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
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-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
i.e. G+, whcih is found only in Archaea at position 15 in the dihydrouridine loop, i.e. D-loop
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
reaction of subunit alpha
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O
L-glutamate + archaeine15 in tRNA
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
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specific Archaea such as Sulfolobus tokodaii have retained ArcS in addition to GAT-QueC, overview
evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
evolution
structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
evolution
the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
evolution
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the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
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evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
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evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
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evolution
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the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
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malfunction
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a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
malfunction
a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
malfunction
recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
malfunction
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recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
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malfunction
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a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
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malfunction
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a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
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malfunction
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recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
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metabolism
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GAT-QueC also catalyzes biosynthesis of G+-tRNA, pathways, overview
metabolism
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TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
metabolism
TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
metabolism
archaeosine biosynthesis pathway, overview
metabolism
archaeosine biosynthesis pathway, overview
metabolism
archaeosine biosynthesis pathway, overview
metabolism
the enzyme is responsible for the final step in the biosynthesis of archaeosine in the D-loop of tRNA
metabolism
-
archaeosine biosynthesis pathway, overview
-
metabolism
-
archaeosine biosynthesis pathway, overview
-
metabolism
-
TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
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metabolism
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archaeosine biosynthesis pathway, overview
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metabolism
-
archaeosine biosynthesis pathway, overview
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metabolism
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archaeosine biosynthesis pathway, overview
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metabolism
-
archaeosine biosynthesis pathway, overview
-
metabolism
-
TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
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metabolism
-
archaeosine biosynthesis pathway, overview
-
metabolism
-
archaeosine biosynthesis pathway, overview
-
metabolism
-
the enzyme is responsible for the final step in the biosynthesis of archaeosine in the D-loop of tRNA
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metabolism
-
archaeosine biosynthesis pathway, overview
-
physiological function
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ArcS catalyzes the final step in the G+ pathway, the conversion of preQ0-tRNA to G+-tRNA, in Euryarchaeota
physiological function
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ArcS catalyzes the final step in the G+ pathway, the conversion of preQ0-tRNA to G+-tRNA, in Euryarchaeota
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
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archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
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physiological function
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archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
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additional information
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G+ can be tolerated in Escherichia coli at position 34 in normally Q-containing tRNA when recombinant GAT-QueC and QueF are introduced
additional information
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presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
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presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
additional information
the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
additional information
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
additional information
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the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
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additional information
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the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
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additional information
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presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
-
additional information
-
the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
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additional information
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Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
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additional information
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the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
-
additional information
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Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-
additional information
-
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
-
additional information
-
the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
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Phillips, G.; Swairjo, M.A.; Gaston, K.W.; Bailly, M.; Limbach, P.A.; Iwata-Reuyl, D.; de Crecy-Lagard, V.
Diversity of archaeosine synthesis in crenarchaeota
ACS Chem. Biol.
7
300-305
2012
no activity in Sulfolobus acidocaldarius, no activity in Pyrobaculum calidifontis, Euryarchaeota, no activity in Pyrobaculum islandicum, Sulfurisphaera tokodaii, Saccharolobus solfataricus (Q981C9), Saccharolobus solfataricus P2 (Q981C9)
brenda
Phillips, G.; Chikwana, V.; Maxwell, A.; El-Yacoubi, B.; Swairjo, M.; Iwata-Reuyl, D.; De Crecy-Lagard, V.
Discovery and characterization of an amidinotransferase involved in the modification of archaeal tRNA
J. Biol. Chem.
285
12706-12713
2010
Haloferax volcanii, Methanocaldococcus jannaschii (Q58428), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58428), Haloferax volcanii H26
brenda
Yokogawa, T.; Nomura, Y.; Yasuda, A.; Ogino, H.; Hiura, K.; Nakada, S.; Oka, N.; Ando, K.; Kawamura, T.; Hirata, A.; Hori, H.; Ohno, S.
Identification of a radical SAM enzyme involved in the synthesis of archaeosine
Nat. Chem. Biol.
15
1148-1155
2019
Thermococcus kodakarensis (Q5JHG7), Methanosarcina acetivorans (Q8TH90), Thermoplasma acidophilum (Q9HJP3), Methanosarcina acetivorans ATCC 35395 (Q8TH90), Thermococcus kodakarensis JCM 12380 (Q5JHG7), Methanosarcina acetivorans DSM 2834 (Q8TH90), Thermoplasma acidophilum JCM 9062 (Q9HJP3), Methanosarcina acetivorans JCM 12185 (Q8TH90), Thermoplasma acidophilum AMRC-C165 (Q9HJP3), Thermococcus kodakarensis ATCC BAA-918 (Q5JHG7), Thermoplasma acidophilum ATCC 25905 (Q9HJP3), Thermoplasma acidophilum NBRC 15155 (Q9HJP3)
brenda
Mei, X.; Alvarez, J.; Bon Ramos, A.; Samanta, U.; Iwata-Reuyl, D.; Swairjo, M.
Crystal structure of the archaeosine synthase QueF-like -Insights into amidino transfer and tRNA recognition by the tunnel fold
Proteins Struct. Funct. Bioinform.
85
103-116
2017
Pyrobaculum calidifontis (A3MSP1), Pyrobaculum calidifontis VA1 (A3MSP1)
brenda