Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA

RNA
Janusz M BujnickiLouis Droogmans

Abstract

The gene encoding the bifunctional enzyme MnmC that catalyzes the two last steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U) in tRNA has been previously mapped at about 50 min on the Escherichia coli K12 chromosome, but to date the identity of the corresponding enzyme has not been correlated with any of the known open reading frames (ORFs). Using the protein fold-recognition approach, we predicted that the 74-kDa product of the yfcK ORF located at 52.6 min and annotated as "putative peptidase" comprises a methyltransferase domain and a FAD-dependent oxidoreductase domain. We have cloned, expressed, and purified the YfcK protein and demonstrated that it catalyzes the formation of mnm5s2U in tRNA. Thus, we suggest to rename YfcK as MnmC.

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Citations

Jul 20, 2006·BMC Molecular Biology·Elzbieta PurtaJanusz M Bujnicki
May 2, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Takuo OsawaTomoyuki Numata
Sep 3, 2011·Microbiology and Molecular Biology Reviews : MMBR·Natalie VerstraetenJan Michiels
Apr 27, 2013·BMC Structural Biology·Jungwook Kim, Steven C Almo
Sep 21, 2011·Briefings in Bioinformatics·Alfonso Benítez-PáezAndrés J Gutiérrez
Oct 14, 2014·International Journal of Molecular Sciences·Daniel C Shippy, Amin A Fadl
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Jun 7, 2014·Frontiers in Genetics·Hiroyuki Hori
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Jun 20, 2017·Archives of Biochemistry and Biophysics·Murielle Lombard, Djemel Hamdane
Sep 27, 2018·RNA Biology·Ismaïl MoukadiriM-Eugenia Armengod
Apr 24, 2019·Chembiochem : a European Journal of Chemical Biology·Nam Y KimJason M Crawford
Jul 10, 2019·IUBMB Life·Emil M Nilsson, Rebecca W Alexander
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Nov 1, 2005·EcoSal Plus·Glenn R Björk, Tord G Hagervall
Jul 12, 2014·BMC Research Notes·Jeanneth Mosquera-RendónAlfonso Benítez-Páez

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