These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of S-adenosylmethionine: ribosomal ribonucleic acid-adenine (N 6 -) methyltransferase of Escherichia coli strain B.
    Author: Sipe JE, Anderson WM, Remy CN, Love SH.
    Journal: J Bacteriol; 1972 Apr; 110(1):81-91. PubMed ID: 4622906.
    Abstract:
    This study is concerned with the isolation and characterization of the enzyme, S-adenosylmethionine:ribosomal ribonucleic acid-adenine (N(6-)) methyl-transferase [rRNA-adenine (N(6)-) methylase] of Escherichia coli strain B, which is responsible for the formation of N(6)-methyladenine moieties in ribosomal ribonucleic acids (rRNA). A 1,500-fold purified preparation of the species-specific methyltransferase methylates a limited number of adenine moieties in heterologous rRNA (Micrococcus lysodeikticus and Bacillus subtilis) and methyl-deficient homologous rRNA. The site recognition mechanism does not require intact 16 or 23S rRNA. The enzyme does not utilize transfer ribonucleic acid as a methyl acceptor nor does it synthesize 2-methyladenine or N(6)-dimethyladenine moieties. Mg(2+), spermine, K(+), and Na(+) increase the reaction rate but not the extent of methylation; elevated concentrations of the cations inhibit markedly. The purified preparations utilize 9-beta-ribosyl-2,6-diaminopurine (DAPR) as a methyl acceptor with the synthesis of 9-beta-ribosyl-6-amino-2-methylaminopurine. A comparison of the two activities demonstrated that one methyltransferase is responsible for the methylation of both DAPR and rRNA. This property provides a sensitive assay procedure unaffected by ribonucleases and independent of any specificity exhibited by rRNA methyl acceptors.
    [Abstract] [Full Text] [Related] [New Search]