Full name: Ribosomal RNA large subunit methyltransferase E
Synonym: RrmJ, Ftsj, MrsF, JW3146
GI: 83287970
Orf: b3179, c3936, z4541, Ecs4058
COG: COG0293
UniProt: P0C0R7
Structures: | 1EIZ | 1EJO |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: l:2552(2552) - Um

Comments:

Substrate analysis showed that RlmE (formerly FtsJ, RrmJ) methylates the 2′-O ribose of the universally conserved U2552 in the so-called A-loop (hairpin 92) of the Peptidyl Transferase Center (domain V) of 23S rRNA. E. coli RlmE is active only on the ribosome and the 50 S ribosomal subunit, but is inactive on free rRNA. AdoMet is the methyl group donor. The enzyme possess a TRAM domain. The homologous S.cerevisiae mitochondrial enzyme is Mrm2. In cytoplasmic large subunit rRNA, the equivalent Um2921 (2552 in E. coli numbering) is catalyzed by C/D box RNP, using snR52 as guide-RNA.

Protein sequence:

MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVV TQIGGKGRIIACDLLPMDPIVGVDFLQGDFRDELVMKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRA MYLVELALEMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP

Enzymatic activities:

Reaction Substrate Type Position
U:Um rRNA (r) LSU/23S/prokaryotic cytosol 2552

Publications:

Title Authors Journal Details PubMed Id DOI
Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. Hager J, Staker BL, Jakob U J Bacteriol [details] 15375145 -
The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase. Caldas T, Binet E, Bouloc P, Costa A, Desgres J, Richarme G J Biol Chem [details] 10748051 -
RNA methylation under heat shock control. Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U Mol Cell [details] 10983982 -
Active site in RrmJ, a heat shock-induced methyltransferase. Hager J, Staker BL, Bugl H, Jakob U J Biol Chem [details] 12181314 -
Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2'-O-methyltransferases. Feder M, Pas J, Wyrwicz LS, Bujnicki JM Gene [details] 12527203 -
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