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Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1982 Jul 25; Vol. 257 (14), pp. 8412-7. - Publication Year :
- 1982
-
Abstract
- A Bacillus subtilis methyltransferase capable of methylating membrane-bound methyl-accepting chemotaxis proteins (MCPs) of a chemotaxis mutant was purified to homogeneity. MCPs are normally unmethylated in this strain. Results of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicate that the enzyme is a 30,000 molecular weight monomer. The enzyme transfers methyl groups from S-adenosylmethionine to glutamate residues of the substrates. The enzyme is activated by divalent cations and has a Km for S-adenosylmethionine of about 5 microM. It is competitively inhibited by S-adenosylhomocysteine, with a Ki of about 0.2 microM, and exhibits an in vitro assay pH optimum of 6.9. This methyltransferase is very different from another methyltransferase from B. subtilis, described previously (Ullah, A. H. J., and Ordal, G. W. (1981) Biochem. J. 199, 795-805).
- Subjects :
- Cations, Divalent
Chemotactic Factors metabolism
Hydrogen-Ion Concentration
Kinetics
Methyl-Accepting Chemotaxis Proteins
Protein O-Methyltransferase metabolism
Bacillus subtilis enzymology
Bacterial Proteins
Chemotactic Factors isolation & purification
Membrane Proteins
Protein Methyltransferases isolation & purification
Protein O-Methyltransferase isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 257
- Issue :
- 14
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6806296