Literature summary for 2.7.7.79 extracted from

Desai, R.; Kim, K.; Buechsenschuetz, H.C.; Chen, A.W.; Bi, Y.; Mann, M.R.; Turk, M.A.; Chung, C.Z.; Heinemann, I.U.
Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase (2018), RNA Biol., 15, 614-622 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene thg1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant enzyme expression	Ignicoccus hospitalis
recombinant expression of only the palm domains from Methanosarcina acetivorans Thg1 (MaPalm, amino acids 1-141)	Methanosarcina acetivorans
recombinant expression of only the palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150)	Pyrobaculum aerophilum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae
Mg2+	required	Ignicoccus hospitalis
Mg2+	required	Pyrobaculum aerophilum
Mg2+	required	Methanosarcina acetivorans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
p-tRNAHis + ATP + GTP + H2O	Saccharomyces cerevisiae	-	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Ignicoccus hospitalis	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Methanosarcina acetivorans	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum DSM 7523	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum IM2	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Saccharomyces cerevisiae ATCC 204508	-	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum NBRC 100827	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum ATCC 51768	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	Pyrobaculum aerophilum JCM 9630	overall reaction	pGp-tRNAHis + AMP + 2 diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Ignicoccus hospitalis	A8A9R6	-	-
Methanosarcina acetivorans	A0A1C7D1G9	-	-
Pyrobaculum aerophilum	Q8ZY97	-	-
Pyrobaculum aerophilum ATCC 51768	Q8ZY97	-	-
Pyrobaculum aerophilum DSM 7523	Q8ZY97	-	-
Pyrobaculum aerophilum IM2	Q8ZY97	-	-
Pyrobaculum aerophilum JCM 9630	Q8ZY97	-	-
Pyrobaculum aerophilum NBRC 100827	Q8ZY97	-	-
Saccharomyces cerevisiae	P53215	-	-
Saccharomyces cerevisiae ATCC 204508	P53215	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme activity assay with purified recombinant palm domains from Methanosarcina acetivorans Thg1 (MaPalm, amino acids 1-141) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. The palm domain of Thg1 is sufficient for catalytic activity	Methanosarcina acetivorans	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum	?	-	-
additional information	the enzyme is active in an in vitro activity assay with radiolabelled Escherichia coli tRNAHisDG-1 and recombinant wild-type IhThg1 enzyme. IhThg1 displays reduced enzyme activity with yeast tRNAHisDG-1, which encodes an A73 discriminator base in compared to Escherichia coli tRNAHisDG-1 with a C73 discriminator base. Radioactive product formation is observed in the presence or absence of ATP, suggesting that IhThg1 does not require ATP-dependent activation, but can utilize GTP, as observed for other archaeal-type Thg1 enzymes. . Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. IhThg1 is active despite lacking conserved RNA recognition motifs. The palm domain of Thg1 is sufficient for catalytic activity	Ignicoccus hospitalis	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum DSM 7523	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum IM2	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum NBRC 100827	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum ATCC 51768	?	-	-
additional information	enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity	Pyrobaculum aerophilum JCM 9630	?	-	-
p-tRNAHis + ATP + GTP + H2O	-	Saccharomyces cerevisiae	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Ignicoccus hospitalis	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Methanosarcina acetivorans	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum DSM 7523	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum IM2	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	-	Saccharomyces cerevisiae ATCC 204508	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum NBRC 100827	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum ATCC 51768	pGp-tRNAHis + AMP + 2 diphosphate	-	?
p-tRNAHis + ATP + GTP + H2O	overall reaction	Pyrobaculum aerophilum JCM 9630	pGp-tRNAHis + AMP + 2 diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
IhThg1	-	Ignicoccus hospitalis
MaThg1	-	Methanosarcina acetivorans
PaThg1	-	Saccharomyces cerevisiae
PaThg1	-	Pyrobaculum aerophilum
THG1	-	Saccharomyces cerevisiae
THG1	-	Ignicoccus hospitalis
THG1	-	Pyrobaculum aerophilum
THG1	-	Methanosarcina acetivorans
Thg1 domain-containing protein	UniProt	Ignicoccus hospitalis
Thg1 domain-containing protein	UniProt	Pyrobaculum aerophilum
tRNA(His)-5'-guanylyltransferase (Thg1) like protein	UniProt	Methanosarcina acetivorans

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Ignicoccus hospitalis

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
37	-	the enzyme is active at 37°C, but not at 65°C	Ignicoccus hospitalis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	archaeal-type Thg1 enzymes are ATP-independent	Pyrobaculum aerophilum
ATP	archaeal-type Thg1 enzymes are ATP-independent	Methanosarcina acetivorans
ATP	archaeal-type Thg1 enzymes are ATP-independent. Product formation is observed in the presence or absence of ATP, suggesting that IhThg1 does not require ATP-dependent activation, but can utilize GTP, as observed for other archaeal-type Thg1 enzymes	Ignicoccus hospitalis
ATP	eukaryotic Thg1 enzymes require ATP for substrate activation	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
evolution	the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1	Saccharomyces cerevisiae
evolution	the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity	Pyrobaculum aerophilum
evolution	the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity	Methanosarcina acetivorans
evolution	the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity. Naturally occurring Thg1 enzyme from Ignicoccus hospitalis (IhThg1) lacks several sections of the protein, and aligns poorly with other Thg1 sequences, it is identified in a large Thg1 phylogenetic analysis	Ignicoccus hospitalis
malfunction	identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization	Saccharomyces cerevisiae
additional information	identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization	Saccharomyces cerevisiae
additional information	Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity	Pyrobaculum aerophilum
additional information	Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity	Methanosarcina acetivorans
additional information	Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity. The catalytic palm domain of IgThg1 can promote forward or reverse extension of a polynucleotide chain and substrate orientation correlates with the direction of polymerization	Ignicoccus hospitalis
physiological function	tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life	Ignicoccus hospitalis
physiological function	tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life	Methanosarcina acetivorans
physiological function	tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. Most eukaryotic Thg1 homologs are essential genes involved in tRNAHis maturation. These enzymes normally catalyze a single 5' guanylation of tRNAHis lacking the essential G-1 identity element required for aminoacylation. G-1 is the critical identity element that histidyl-tRNA synthetase (HisRS) uses to recognize its cognate tRNA, enabling HisRS to differentiate tRNAHis from the pool of other cellular tRNAs	Saccharomyces cerevisiae
physiological function	tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products	Pyrobaculum aerophilum

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Release 2023.1 (January 2023)