期刊
FEMS MICROBIOLOGY LETTERS
卷 318, 期 1, 页码 1-9出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2011.02228.x
关键词
secretion system; motility; peptidoglycan; twitching; swimming; toxin
类别
资金
- Natural Sciences and Engineering Research Council
- Advanced Food and Materials Network of Centres of Excellence
- Canadian Institutes of Health Research (CIHR)
Peptidoglycan plays a vital role in bacterial physiology, maintaining cell shape and resisting cellular lysis from high internal turgor pressures. Its integrity is carefully maintained by controlled remodeling during growth and division by the coordinated activities of penicillin-binding proteins, lytic transglycosylases, and N-acetylmuramyl-l-alanine amidases. However, its small pore size (similar to 2 nm) and covalently closed structure make it a formidable barrier to the assembly of large macromolecular cell-envelope-spanning complexes involved in motility and secretion. Here, we review the strategies used by Gram-negative bacteria to assemble such macromolecular complexes across the peptidoglycan layer, while preserving its essential structural role. In addition, we discuss evidence that suggests that peptidoglycan can be integrated into cell-envelope-spanning complexes as a structural and functional extension of their architecture.
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