Open AccessSite-Directed Mutagenesis Identifies a Molecular Switch Involved in Copper Sensing by the Histidine Kinase CinS in Pseudomonas putida KT2440
Author(s) -
Davide Quaranta,
Megan M. McEvoy,
Christopher Rensing
Publication year - 2009
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.00551-09
Subject(s) - pseudomonas putida , biology , mutant , mutagenesis , copper , histidine kinase , histidine , biochemistry , bacteria , microbiology and biotechnology , genetics , gene , enzyme , chemistry , organic chemistry
In the presence of copper,Pseudomonas putida activates transcription ofcinAQ via the two-component system CinS-CinR. The CinS-CinR TCS was responsive to 0.5 μM copper and was specifically activated only by copper and silver. Modeling studies of CinS identified a potential copper binding site containing H37 and H147. CinS mutants with H37R and H147R mutations had an almost 10-fold reduced copper-dependent induction ofcinAQ compared to the wild type.