Protein Summary

RlmJ from Escherichia coli

Full name: Ribosomal RNA large subunit methyltransferase J
Synonym: yhiR
GI: 586675
Orf: b3499, JW3466
COG: COG2961
UniProt: P37634
Structures: | 4BLW | 4BLV | 4BLU |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: l:2030(2030) - m6A

Comments:

SAM-dependent MTase. The enzyme is neither essential for ribosome assembly nor for function. The substrate preference in vitro is deproteinized 23S rRNA. Modified residue m6A2030 is located in helix 72, close the peptidyltransferase center of Domain IV and the elongation factor binding site of Domain II in the folded 3D architecture of the ribosome. Orthologs are found mostly in proteobacteria. A possible role is stabilization of local tertiary structure of the ribosome. M6A exist also at position 1618 where it is introduced by a related MTase RlmF(UbiN) and of course at the conserved m6,2A1518, 1519 of 16S rRNA (introduced by RsmA/KsgA).

Protein sequence:

MLSYRHSFHAGNHADVLKHTVQSLIIESLKEKDKPFLYLDTHAGAGRYQL
GSEHAERTGEYLEGIARIWQQDDLPAELEAYINVVKHFNRSGQLRYYPGS
PLIARLLLREQDSLQLTELHPSDYPLLRSEFQKDSRARVEKADGFQQLKA
KLPPVSRRGLILIDPPYEMKTDYQAVVSGIAEGYKRFATGIYALWYPVVL
RQQIKRMIHDLEATGIRKILQIELAVLPDSDRRGMTASGMIVINPPWKLE
QQMNNVLPWLHSKLVPAGTGHATVSWIVPE

Enzymatic activities

Reaction Substrate Type Position
A:m6A rRNA (r) LSU/23S/prokaryotic cytosol 2030

Publications

Title Authors Journal Details PubMed Id DOI
The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA. Golovina AY, Dzama MM, Osterman IA, Sergiev PV, Serebryakova MV, Bogdanov AA, Dontsova OA... RNA [details] 22847818 -
Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ. Punekar AS, Liljeruhm J, Shepherd TR, Forster AC, Selmer M... Nucleic Acids Res [details] 23945937 -

Links

_EcoCyc_
_PubMed_

Last modification of this entry: 2013-09-19 12:42:28.472326
Edited by a user: magda
Edited content: No fields changed.