Mur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain

Citation
C. Husson-kao et al., Mur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain, FEMS MICROB, 187(1), 2000, pp. 69-76
Citations number
19
Categorie Soggetti
Microbiology
Journal title
FEMS MICROBIOLOGY LETTERS
ISSN journal
03781097 → ACNP
Volume
187
Issue
1
Year of publication
2000
Pages
69 - 76
Database
ISI
SICI code
0378-1097(20000601)187:1<69:MASTPH>2.0.ZU;2-Q
Abstract
The gene encoding Mur1, a Streptococcus thermophilus peptidoglycan hydrolas e, 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. S equence analysis evidenced that Mur1 encompasses exactly the AcmA region co ntaining the catalytic domain, but lacks the one containing amino acid repe ats involved in cell wall binding. Mur1 appears to be expressed and cell-as sociated in S. thermophilus. as revealed by immunoblot analysis. These resu lts suggest that the cell wall attachment mode of Mur1 differs from that of most peptidoglycan hydrolases described so far. (C) 2000 Federation of Eur opean Microbiological Societies. Published by Elsevier Science B.V. All rig hts reserved.