Mutational analysis of basic residues in the N-terminus of the rRNA:m6A methyltransferase ErmC'
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15114858
DOI
10.1007/bf02931637
Knihovny.cz E-resources
- MeSH
- Amino Acids, Basic genetics MeSH
- Anti-Bacterial Agents pharmacology MeSH
- Bacillus subtilis enzymology genetics MeSH
- Drug Resistance, Bacterial genetics MeSH
- RNA, Bacterial metabolism MeSH
- DNA, Bacterial genetics physiology MeSH
- Erythromycin pharmacology MeSH
- Conserved Sequence MeSH
- Methyltransferases genetics isolation & purification metabolism physiology MeSH
- Microbial Sensitivity Tests MeSH
- Molecular Sequence Data MeSH
- Mutagenesis, Site-Directed MeSH
- Oligoribonucleotides metabolism MeSH
- Frameshift Mutation MeSH
- RNA, Ribosomal, 23S metabolism MeSH
- S-Adenosylmethionine metabolism MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amino Acids, Basic MeSH
- Anti-Bacterial Agents MeSH
- RNA, Bacterial MeSH
- DNA, Bacterial MeSH
- Erythromycin MeSH
- Methyltransferases MeSH
- Oligoribonucleotides MeSH
- RNA, Ribosomal, 23S MeSH
- rRNA (adenosine-O-2'-)methyltransferase MeSH Browser
- S-Adenosylmethionine MeSH
Erm methyltransferases mediate the resistance to the macrolide-lincosamide-streptogramin B antibiotics via dimethylation of a specific adenine residue in 23S rRNA. The role of positively charged N-terminal residues of the ErmC' methyltransferase in RNA binding and/or catalysis was determined. Mutational analysis of amino acids K4 and K7 was performed and the mutants were characterized in in vivo and in vitro experiments. The K4 and K7 residues were suggested not to be essential for the enzyme activity but to provide a considerable support for the catalytic step of the reaction, probably by maintaining the optimum conformation of the transition state through interactions with the phosphate backbone of RNA.
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