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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

TRM5 tRNA methyltransferase 5 homolog

tRNA methyltransferase, Trm5, KIAA1393, tRNA (guanine-N(1)-)-methyltransferase, m1G methyltransferase
tRNAs contain as many as 13 or 14 nucleotides that are modified posttranscriptionally by enzymes that are highly specific for particular nucleotides in the tRNA structure. TRMT5 methylates the N1 position of guanosine-37 (G37) in selected tRNAs using S-adenosyl methionine (Brule et al., 2004 [PubMed 15248782]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, AdoMet, TRM1, MET2
Papers on tRNA methyltransferase
NSun2 delays replicative senescence by repressing p27 (KIP1) translation and elevating CDK1 translation.
Wang et al., Beijing, China. In Aging (albany Ny), Jan 2016
Here, we show that the tRNA methyltransferase NSun2 represses the expression of p27 in replicative senescence.
Trm9-Catalyzed tRNA Modifications Regulate Global Protein Expression by Codon-Biased Translation.
Dedon et al., Albany, United States. In Plos Genet, Dec 2015
Here we use quantitative proteomics to show a direct link between wobble uridine 5-methoxycarbonylmethyl (mcm5) and 5-methoxy-carbonyl-methyl-2-thio (mcm5s2) modifications catalyzed by tRNA methyltransferase 9 (Trm9) in tRNAArg(UCU) and tRNAGlu(UUC) and selective translation of proteins from genes enriched with their cognate codons.
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Pearson et al., Dundee, United Kingdom. In Diabet Med, Dec 2015
BACKGROUND: A syndrome of young-onset diabetes mellitus associated with microcephaly, epilepsy and intellectual disability caused by mutations in the tRNA methyltransferase 10 homologue A (TRMT10A) gene has recently been described.
Blind Pose Prediction, Scoring, and Affinity Ranking of the CSAR 2014 Dataset.
Iorga et al., Gif-sur-Yvette, France. In J Chem Inf Model, Nov 2015
UNASSIGNED: The 2014 CSAR Benchmark Exercise was focused on three protein targets: coagulation factor Xa, spleen tyrosine kinase, and bacterial tRNA methyltransferase.
Loss of a Conserved tRNA Anticodon Modification Perturbs Plant Immunity.
Vera et al., Valencia, Spain. In Plos Genet, Oct 2015
Our results reveal SCS9 encodes a tRNA methyltransferase that mediates the 2´-O-ribose methylation of selected tRNA species in the anticodon loop.
The tRNA methyltransferase Dnmt2 is required for accurate polypeptide synthesis during haematopoiesis.
Lyko et al., Heidelberg, Germany. In Embo J, Oct 2015
The Dnmt2 enzyme utilizes the catalytic mechanism of eukaryotic DNA methyltransferases to methylate several tRNAs at cytosine 38.
Application of Shape Similarity in Pose Selection and Virtual Screening in CSARdock2014 Exercise.
Zhang et al., Yokohama, Japan. In J Chem Inf Model, Sep 2015
UNASSIGNED: To evaluate the applicability of shape similarity in docking-based pose selection and virtual screening, we participated in the CSARdock2014 benchmark exercise for identifying the correct docking pose of inhibitors targeting factor XA, spleen tyrosine kinase, and tRNA methyltransferase.
Kinetic Analysis of tRNA Methyltransferases.
Masuda et al., Philadelphia, United States. In Methods Enzymol, 2014
This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea.
Diversity in mechanism and function of tRNA methyltransferases.
Jackman et al., Columbus, United States. In Rna Biol, 2014
Here we review recent advances in tRNA methyltransferase mechanism and function with a particular emphasis on discoveries of alternative substrate specificities and chemistry associated with some methyltransferases.
The Role of a Novel TRMT1 Gene Mutation and Rare GRM1 Gene Defect in Intellectual Disability in Two Azeri Families.
Najmabadi et al., Tehrān, Iran. In Plos One, 2014
Conversely, the TRMT1 gene encodes a tRNA methyltransferase that dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl methionine as the methyl group donor.
tRNA modifications regulate translation during cellular stress.
Dedon et al., Cambridge, United States. In Febs Lett, 2014
In support of this general model of translational control of stress response, studies making use of detailed measures of translation, tRNA methyltransferase mutants, and computational and mass spectrometry approaches reveal that stress reprograms tRNA modifications to translationally regulate MoTTs linked to arginine and leucine codons, which helps cells survive insults by damaging agents.
Roles of 17β-hydroxysteroid dehydrogenase type 10 in neurodegenerative disorders.
Philipp et al., United States. In J Steroid Biochem Mol Biol, 2014
This enzyme is capable of binding to other peptides, such as estrogen receptor α, amyloid-β, and tRNA methyltransferase 10C.
RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme.
Rossmanith et al., Vienna, Austria. In Cell, 2008
Moreover, the mitochondrial enzyme turns out to be an unexpected type of patchwork enzyme, composed of a tRNA methyltransferase, a short-chain dehydrogenase/reductase-family member, and a protein of hitherto unknown functional and evolutionary origin, possibly representing the enzyme's metallonuclease moiety.
Identification and characterization of modification enzymes by biochemical analysis of the proteome.
Phizicky et al., Rochester, United States. In Methods Enzymol, 2006
Here we describe a generalized procedure for the biochemical analysis of a yeast proteomic library for identification of nucleic acid-modifying enzymes, by use of the yeast MORF (Moveable Open Reading Frame) library (Gelperin et al., 2005) as the source of protein activity, and the known yeast tRNA methyltransferase Trm4 as a test case.
Two substrates are better than one: dual specificities for Dnmt2 methyltransferases.
Lyko et al., Bremen, Germany. In Trends Biochem Sci, 2006
Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.
Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein.
Holmes et al., Richmond, United States. In Biochemistry, 2004
comparison of human TRM5 and E Coli TrmD activities, requirements for optimal activity, and tRNA methylation sites
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