Open AccessMur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain
Author(s) -
HussonKao Clara,
Mengaud Jérôme,
Benbadis Laurent,
ChapotChartier MariePierre
Publication year - 2000
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.1574-6968.2000.tb09139.x
Subject(s) - autolysin , peptidoglycan , lactococcus lactis , lysin , cell wall , biology , streptococcus thermophilus , hydrolase , biochemistry , signal peptide , gene , peptide sequence , microbiology and biotechnology , enzyme , genetics , bacteriophage , bacteria , escherichia coli , lactic acid , fermentation , lactobacillus
The gene encoding Mur1, a Streptococcus thermophilus peptidoglycan hydrolase, was cloned by homology with acmA , the Lactococcus lactis major autolysin gene. Mur1 is a 24.7‐kDa protein endowed with a putative signal peptide. Sequence analysis evidenced that Mur1 encompasses exactly the AcmA region containing the catalytic domain, but lacks the one containing amino acid repeats involved in cell wall binding. Mur1 appears to be expressed and cell‐associated in S. thermophilus , as revealed by immunoblot analysis. These results suggest that the cell wall attachment mode of Mur1 differs from that of most peptidoglycan hydrolases described so far.