Open AccessEscherichia coli recA gene product inactivates phage lambda repressor.
Author(s) -
Jeffrey W. Roberts,
Charles W.M. Roberts,
Nancy L. Craig
Publication year - 1978
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.10.4714
Subject(s) - escherichia coli , repressor , lambda phage , biology , bacteriophage , gene , microbiology and biotechnology , gene product , sos response , chemistry , gene expression , biochemistry
Phage lambda repressor is inactivated and cleaved into two detectable fragments during incubation with purified Escherichia coli recA gene protein in vitro, in a reaction that requires ATP. This reaction reproduces the recA-dependent inactivation of repressor that occurs in vivo during induction of the SOS functions. The proteolytic activity may reside in the recA protein itself and may be a fundamental activity of it.
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