| Literature DB >> 794833 |
H J Aschhoff, H Elten, H H Arnold, G Mahal, W Kersten, H Kersten.
Abstract
A 7-methylguanine (m7G) specific tRNA methyltransferase from E. coli MRE 600 was purified about 1000 fold by affinity chromatography on Sepharose bound with normal E. coli tRNA. The purified enzyme catalyzes exclusively the formation of m7G in submethylated bulk tRNA of E. coli K12 met- rel-. The purified enzyme transfers the methyl group from S-adenosyl-methionine to initiator tRNA of B. subtilis and 0.8 moles m7G residues are formed per mole tRNA. It is suggested that the enzyme specifically recognizes the extra arm unpaired guanylate residue.Entities:
Mesh：
Substances：
Year: 1976 PMID： 794833 PMCID： PMC343155 DOI： 10.1093/nar/3.11.3109
Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971