The enzyme from Saccharomyces cerevisiae specifically methylates guanine9 [1,2]. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of adenine9 in tRNA (cf. EC 2.1.1.218, tRNA (adenine9-N1)-methyltransferase) [1].
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea. The tRNA methyltransferase Trm10 is a highly conserved protein both necessary and sufficient to catalyze all known instances of m1G9 modification in yeast
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
TRMT10A silencing induces human beta-cell apoptosis.. TRMT10A deficiency negatively affects beta-cell mass and the pool of neurons in the developing brain. A nonsense mutation R127stop in the enzyme is involved in the syndrome of young onset diabetes, short stature and microcephaly (small brain size) with intellectual disability in a large consanguineous family, TRMT10A mRNA and protein are absent in cells from affected siblings, phenotype, overview. Patients are homozygous for a nonsense mutation in TRMT10A and lose TRMT10A expression
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
formation of N1-methylguanine9 in tRNA(Asp) from Thermococcus kodakaraensis that contains a guanosine at position 9. The enzyme forms approximately the same amount of m1A and m1G when the tRNA of the yeast strain Y16243 is used as substrate. Given that occurrence of A9 and G9 in this tRNA population is almost equal (about 50% each) this result indicates that the enzyme TK0422p does not show any preference for one of these two nucleosides. The ratio m1A/m1G formed from Escherichia coli tRNA is higher than that with tRNA from the yeast Y16243 strain. This is consistent with the fact that there are about two times more tRNAs with A9 than with G9 in Escherichia coli. The enzyme is active in a pH range 5.5-9.75. The intensity of m1A and m1G spots varies greatly as a function of the pH. At pH 5.5, m1A MTase activity of TK0422p is predominant over m1G. At pH 7 or higher, both m1A and m1G are detected, m1G intensity growing with increasing pH
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
the bifunctional enzyme is active in a pH range 5.5-9.75. The intensity of m1A and m1G spots varies greatly as a function of the pH. At pH 5.5, m1A MTase activity of TK0422p is predominant over m1G. At pH 7 or higher, both m1A and m1G are detected, m1G intensity growing with increasing pH
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
purified enzyme free or in complex with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 2.0-2.5 A resolution, molecular replacement
recombinant N-terminally His-tagged enzyme Trm10 from Escherichia coli strain BL21/Gold(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography, followed by dialysis
recombinant N-terminally His-tagged enzyme Trm10 from Escherichia coli strain BL21/Gold(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography, followed by dialysis. Purification of the recombinant TrmT10C-SDR5C1 wild-type and mutant complexes by nickel affinity chromatography
recombinant expression of N-terminally His-tagged enzyme Trm10 in Escherichia coli strain BL21/Gold(DE3), selenomethionine-labeled spTrm10_74 (residues 74-281) is expressed in Escherichia coli strain B834, recombinant wild-type and mutant Q226A TrmT10C (residues 40-403) is coexpressed with His-tagged protein SDR5C1
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Case Report: Compound heterozygous nonsense mutations in TRMT10A are associated with microcephaly, delayed development, and periventricular white matter hyperintensities.
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.
Homozygous deletion of TRMT10A as part of a contiguous gene deletion in a syndrome of failure to thrive, delayed puberty, intellectual disability and diabetes mellitus.