Protein Variants | Comment | Organism |
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additional information | Saccharomyces cerevisiae tRNAHis transcripts with and without G-1 are generated, carrying a C73 discriminator instead of the wild-type A73 position (tRNAHisDELTAG-1 A73C and tRNAHis+G-1 A73C). Due to the additional base pair G-1/C73, tRNAHis+G-1 A73C carries an extended acceptor stem with a base-paired discriminator position. This situation does not affect CCA-addition catalyzed by the CCA-adding enzyme and results in a similarly efficient CCA incorporation to tRNAHis+G-1 A73C compared to tRNAHisDELTAG-1 A73C. Both tRNAHis substrates with a cytosine at the discriminator position are readily accepted as substrates for CCA-addition, showing comparable band patterns like the wild-type tRNAHis containing an A73. Analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
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additional information | - |
additional information | analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
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Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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p-tRNAHis + ATP + GTP + H2O | Saccharomyces cerevisiae | overall reaction | pGp-tRNAHis + AMP + 2 diphosphate | - |
? | |
p-tRNAHis + ATP + GTP + H2O | Saccharomyces cerevisiae ATCC 204508 | overall reaction | pGp-tRNAHis + AMP + 2 diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | P53215 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P53215 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. On the substrate lacking the CCA-end (tRNAHisDELTACCA), the enzyme is less efficient | Saccharomyces cerevisiae | ? | - |
- |
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additional information | tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. On the substrate lacking the CCA-end (tRNAHisDELTACCA), the enzyme is less efficient | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
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p-tRNAHis + ATP + GTP + H2O | overall reaction | Saccharomyces cerevisiae | pGp-tRNAHis + AMP + 2 diphosphate | - |
? | |
p-tRNAHis + ATP + GTP + H2O | overall reaction | Saccharomyces cerevisiae ATCC 204508 | pGp-tRNAHis + AMP + 2 diphosphate | - |
? |
Synonyms | Comment | Organism |
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THG1 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
metabolism | in eukaryotes including yeast, both 3'-CCA and 5'-G-1 are added posttranscriptionally by tRNA nucleotidyltransferase and tRNAHis guanylyltransferase, respectively. These two cytosolic enzymes might compete for the same tRNA, but tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. Thus, although many tRNA maturation steps can occur in a rather random order, pathway where CCA-addition precedes G-1 incorporation is likely in Saccharomyces cerevisiae. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. Sequential order of tRNAHis processing, overview. The enzymes do not compete for the substrate. Instead, the differing substrate preferences lead to a sequential order of nucleotide incorporation at 5'- and 3'-ends, resulting in a mature tRNAHis in the cytosol | Saccharomyces cerevisiae |
physiological function | the tRNAHis guanylyltransferase posttranscriptionally adds a 5'-G-1 from GTP to yeast tRNAHis. The presence of this single G at the -1 position is critical for recognition of tRNAHis by the histidyl-tRNA synthetase (HisRS). Thg1 adds a single G-1 residue across from an A73 discriminator nucleotide, forming an unconventional non-Watson Crick base pair. This unusual 3'-5' nucleotidyltransferase protein is a member of a larger family of Watson Crick-dependent 3'-5' polymerase enzymes that share structural similarity with canonical 5'-3' DNA and RNA polymerases | Saccharomyces cerevisiae |