Enter Your Search:
Results 1-2 (2)
Go to page number:
Select a Filter Below
Nucleic Acids Research (1)
RNA Biology (1)
Auxilien, Sylvie (2)
Golinelli-Pimpaneau, Béatrice (2)
Armengaud, Jean (1)
Bujnicki, Janusz M. (1)
Chaussinand, Guylaine (1)
Dedieu, Alain (1)
Fernandez, Bernard (1)
Gabant, Guillaume (1)
Gajda, Michal J. (1)
Grosjean, Henri (1)
Guérineau, Vincent (1)
Locard, Marie (1)
Szweykowska-Kulińska, Zofia (1)
Tuszynska, Irina (1)
Year of Publication
Did you mean:
The human tRNA m5C methyltransferase Misu is multisite-specific
The human tRNA m5C methyltransferase Misu is a novel downstream target of the proto-oncogene Myc that participates in controlling cell division and proliferation. Misu catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to carbon 5 of cytosines in tRNAs. It was previously shown to catalyze in vitro the intron-dependent formation of m5C at the first position of the anticodon (position 34) within the human pre-tRNALeu(CAA). In addition, it was recently reported that C48 and C49 are methylated in vivo by Misu. We report here the expression of hMisu in Escherichia coli and its purification to homogeneity. We show that this enzyme methylates position 48 in tRNALeu(CAA) with or without intron and positions 48, 49 and 50 in tRNAGly2(GCC) in vitro. Therefore, hMisu is the enzyme responsible for the methylation of at least four cytosines in human tRNAs. By comparison, the orthologous yeast enzyme Trm4 catalyzes the methylation of carbon 5 of cytosine at positions 34, 40, 48 or 49 depending on the tRNAs.
tRNA modification enzyme; RNA methyltransferase; 5-methylcytosine; m5C; Misu; NSun2; Trm4
THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously folding domain
Gajda, Michal J.
Bujnicki, Janusz M.
Nucleic Acids Research
The tRNA:m22G10 methyltransferase of Pyrococus abyssi (PAB1283, a member of COG1041) catalyzes the N2,N2-dimethylation of guanosine at position 10 in tRNA. Boundaries of its THUMP (THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases)—containing N-terminal domain [1–152] and C-terminal catalytic domain [157–329] were assessed by trypsin limited proteolysis. An inter-domain flexible region of at least six residues was revealed. The N-terminal domain was then produced as a standalone protein (THUMPα) and further characterized. This autonomously folded unit exhibits very low affinity for tRNA. Using protein fold-recognition (FR) methods, we identified the similarity between THUMPα and a putative RNA-recognition module observed in the crystal structure of another THUMP-containing protein (ThiI thiolase of Bacillus anthracis). A comparative model of THUMPα structure was generated, which fulfills experimentally defined restraints, i.e. chemical modification of surface exposed residues assessed by mass spectrometry, and identification of an intramolecular disulfide bridge. A model of the whole PAB1283 enzyme docked onto its tRNAAsp substrate suggests that the THUMP module specifically takes support on the co-axially stacked helices of T-arm and acceptor stem of tRNA and, together with the catalytic domain, screw-clamp structured tRNA. We propose that this mode of interactions may be common to other THUMP-containing enzymes that specifically modify nucleotides in the 3D-core of tRNA.
Results 1-2 (2)
Go to page number:
Remove citation from clipboard
Add citation to clipboard
This will clear all selections from your clipboard. Do you wish proceed?
Clipboard is full! Please remove an item and try again.
PubMed Central Canada is a service of the
Canadian Institutes of Health Research
(CIHR) working in partnership with the National Research Council's
Canada Institute for Scientific and Technical Information
in cooperation with the
National Center for Biotechnology Information
U.S. National Library of Medicine
(NCBI/NLM). It includes content provided to the
PubMed Central International archive
by participating publishers.