MiaB from Escherichia coli - protein summary.
tRNA (N6-isopentenyl adenosine(37)-C2)-methylthiotransferase
Position of modification - modification:
t:37 - ms2i6A
Bacterial MiaB works on A36-i6A37-containing tRNA. It displays a N-terminal TRAM domain and a C-terminal catalytic radical SAM domain with two [4Fe-4S] clusters coordinated with 3 cysteines and an exchangeable S-AdoMet. It works with IcsS/IcsU as the donor of sulfur. Belongs to the same family of methylthiotransferases as B subtilis MTaB (YqeV), mammalian MtaB (Cdkal1) and protein methylthiotransferase RimO. A MiaB-CDKAL1-like enzyme is present in Archaea, while MiaA/Mod5 is totally absent. Its function is still elusive (2012). MnmE-GTpase negatively regulates the activity of MiaG in E. coli.
MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA.
Pierrel F, Douki T, Fontecave M, Atta M
J Biol Chem
Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli.
Esberg B, Leung HC, Tsui HC, Bjork GR, Winkler ME
Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar Typhimurium occurs in two principally distinct pathways.
Leipuviene R, Qian Q, Bjork GR
Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.
Pierrel F, Bjork GR, Fontecave M, Atta M
J Biol Chem
Evidence that the folate-dependent proteins YgfZ and MnmEG have opposing effects on growth and on activity of the iron-sulfur enzyme MiaB.
Waller JC, Ellens KW, Hasnain G, Alvarez S, Rocca JR, Hanson AD
TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes.
Anantharaman V, Koonin EV, Aravind L
FEMS Microbiol Lett
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