Open AccessFunctioning of the cloned phage MS2 lysis protein in Escherichia coli impaired in murein synthesis
Author(s) -
UrsinusWössner Astrid,
Höltje JoachimVolker
Publication year - 1989
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.1574-6968.1989.tb03224.x
Subject(s) - lysis , mecillinam , escherichia coli , biology , penicillin binding proteins , mutant , lysin , biochemistry , peptidoglycan , microbiology and biotechnology , bacteriophage ms2 , bacteriophage , enterobacteriaceae , cell wall , gene
The mode of action of the phage MS2 lysis protein seems not to involve a direct interaction with the murein synthesis machinery as is the case for lysis induced by β‐lactam antibiotics. Mutants with defects in various penicillin‐binding proteins, which are involved in murein synthesis, were found to show normal lysis sensitivity towards the cloned MS2 lysis protein. In addition, both processes, longitudinal growth of the murein sacculus in the presence of furazlocillin, cephalexin and nalidixic acid as well as spherical growth in the presence of mecillinam were sensitive to the phage lysis protein. No change in the capacity of the binding proteins to bind 14 C‐labelled penicillin G was observed in the presence of the MS2 lysis gene product.