Open AccessMolecular characterization of two cya mutations, cya-854 and cyaR1
Author(s) -
Philippe Glaser,
A. K. Roy,
Antoine Danchin
Publication year - 1989
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.171.9.5176-5178.1989
Subject(s) - biology , escherichia coli , mutation , genetics , adenylate kinase , cyclase , base pair , dna , gene , receptor
The cya-854 mutation of Escherichia coli K-12 (E. Brickman, L. Soll, and J. Beckwith, J. Bacteriol. 116:582-587, 1973) has been shown to consist of a 200-base-pair deletion generating a new translation start that permits synthesis of the adenylate cyclase carboxy terminus. Contrary to expectations (C. Guidi-Rontani, A. Danchin, and A. Ullmann, J. Bacteriol. 148:753-761, 1981), cyaR1 results from the insertion of an IS1 element into the sequence coding for the catalytic center of the protein.