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Literature summary for 2.1.1.214 extracted from

  • Mazauric, M.H.; Dirick, L.; Purushothaman, S.K.; Björk, G.R.; Lapeyre, B.
    Trm112p is a 15-kDa zinc finger protein essential for the activity of two tRNA and one protein methyltransferases in yeast (2010), J. Biol. Chem., 285, 18505-18515.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene TRM112, phylogenetic analysis, expression of His-tagged Trm112p, alone or with Trm9p, in Escherichia coli strain S15 (DE3-pLysS), Trm112p forms a complex with Trm9p, which renders the latter soluble Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information a plasmid containing a wild-type copy of the TRM112 gene (pBL652) is able to restore the formation of the two modified nucleosides in a trm112-0 strain Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine10 in tRNA Saccharomyces cerevisiae
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S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged Trm112p, alone or with Trm9p, from Escherichia coli strain S15 (DE3-pLysS) by nickel affinity chromatography and desalting gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine10 in tRNA
-
Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
?

Subunits

Subunits Comment Organism
More Trm112p is a small 15-kDa protein that contains a zinc finger domain, a motif composed of four cysteines arranged with a certain spacing, which can form a secondary structure resembling a finger Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Trmp112p
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Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction TRM112 mutant strains show growth defects, as well as nuclear genomic instability and mitotic defects, overview. Chromosome instability increases 6-7-fold in trm112-0 compared with wild-type. trm112-0 strain is resistant to zymocin, thetRNase toxin produced by Kluyveromyces lactis that specifically targets the mcm5s2U modification at position 34 and cleaves tRNAUUGGln, tRNAUUCGlu, and tRNAUUU Saccharomyces cerevisiae
physiological function Trm11p and Trm112p are two interacting proteins that are both required for catalyzing the formation of m2G at position 10 in several tRNAs. Trm11p is the catalytic subunit, but also Trm112p is essential for the formation of m2G10, Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, because Trm112p is capable of directing the proper folding of Trm11p, leading to the synthesis of an active complex. Trm112p is required in vivo for the formation of mcm5U34 and mcm5s2U34, overview. Trm112p is also required for the activity of Mtq2p, a protein methyltransferase that catalyzes the methylation of the glutamine of the universally conserved GGQ tripeptide of the translation termination factor eRF1/Sup45. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell Saccharomyces cerevisiae