Open AccessExpression in Escherichia coli of the carboxy terminal domain of the BLAR sensory‐transducer protein of Bacillus licheniformis as a water‐soluble M r 26 000 penicillin‐binding protein
Author(s) -
Joris B.,
Ledent P.,
Kobayashi T.,
Lampen J.O.,
Ghuysen J.M.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03785.x
Subject(s) - periplasmic space , escherichia coli , bacillus licheniformis , bacillus subtilis , chemotaxis , homology (biology) , chemistry , biology , biochemistry , bacteria , amino acid , gene , genetics , receptor
A cloning vector has been constructed which allows production and export by Escherichia coli of the Met346‐Arg601 carboxy terminal domain of the 601 aminoc acid BLAR sensory‐transducer involved in ß‐lactamase inducibility in Bacillus Licheniformis . The polypeptide, referred to as BLAR‐CTD, accumulates in the periplasm of E. coli in the form of a water‐soluble, M r 26 000 penicillin‐binding protein. These data and homology searches suggest that BLAR has a membrane topology similar to that of other sensory‐transducers involved in chemotaxis.