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MTQ2 Mtq2p

Mtq2, Mtq2p, N6-DNA-methyltransferase, HemK2
This gene encodes protein methyltransferase. The encoded enzyme may be involved in the methylation of release factor I during translation termination. This enzyme is also involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 11. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: IRF, OUT, ACID, CAN, fibrillin-1
Papers on Mtq2
Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) in arsenic biomethylation and its role in arsenic-induced toxicity.
Zhang et al., Berkeley, United States. In Environ Health Perspect, 2011
N6AMT1 converted monomethylarsonous acid to dimethylarsonic acid when overexpressed in UROtsa human urothelial cells. It is expressed in many human tissues at variable levels, supporting a potential participation in arsenic metabolism in vivo.
Trm112p is a 15-kDa zinc finger protein essential for the activity of two tRNA and one protein methyltransferases in yeast.
Lapeyre et al., Montpellier, France. In J Biol Chem, 2010
Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, and for Mtq2p, an enzyme that methylates the translation termination factor eRF1/Sup45.
Changing the DNA recognition specificity of the EcoDam DNA-(adenine-N6)-methyltransferase by directed evolution.
Jeltsch et al., Bremen, Germany. In J Mol Biol, 2010
EcoDam is an adenine-N6 DNA methyltransferase that methylates the GATC sites in the Escherichia coli genome.
tRNA and protein methylase complexes mediate zymocin toxicity in yeast.
Schaffrath et al., Halle, Germany. In Mol Microbiol, 2008
Most strikingly, C-terminal truncations in Trm9 abolish interaction with Trm112, a protein shown to individually purify with Lys9 and two more methylases, Trm11 and Mtq2.
HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1.
Heurgué-Hamard et al., Paris, France. In Febs Lett, 2008
The human HemK2 protein methylates human and yeast eRF1.eRF3.GTP in vitro, and that the methyltransferase catalytic subunit can complement the growth defect of yeast strains deleted for mtq2.
The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.
Sherman et al., Rochester, United States. In J Biol Chem, 2006
Mtq2p methylates Sup45p the mtq2-Delta had multiple phenotypes, including cold sensitivity and sensitivity to translation fidelity antibiotics paromomycin and geneticin, to high salt and calcium concentrations, to polymyxin B, and to caffeine
The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene.
Buckingham et al., Paris, France. In J Biol Chem, 2005
the natural substrate of the methyltransferase YDR140w is the ternary complex eRF1.eRF3.GTP
Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase.
Friedrich et al., Gießen, Germany. In J Mol Biol, 1999
DNA methyltransferases flip their target base out of the DNA helix.
Sequence-specific recognition of cytosine C5 and adenine N6 DNA methyltransferases requires different deformations of DNA.
Reich et al., Santa Barbara, United States. In Proc Natl Acad Sci U S A, 1996
In contrast, similar analysis of M.EcoRI, an adenine N6 DNA methyltransferase, shows an average bend angle of approximately 52 degrees.
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