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The cell wall amidase AmiB is essential for P seudomonas aeruginosa cell division, drug resistance and viability
Author(s) -
Yakhnina Anastasiya A.,
McManus Heather R.,
Bernhardt Thomas G.
Publication year - 2015
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13077
Subject(s) - biology , amidase , cell division , cell envelope , microbiology and biotechnology , pseudomonas aeruginosa , cell , peptidoglycan , bacterial cell structure , cell wall , biochemistry , escherichia coli , bacteria , genetics , enzyme , gene
Summary The physiological function of cell wall amidases has been investigated in several proteobacterial species. In all cases, they have been implicated in the cleavage of cell wall material synthesized by the cytokinetic ring. Although typically non‐essential, this activity is critical for daughter cell separation and outer membrane invagination during division. In E scherichia coli , proteins with LytM domains also participate in cell separation by stimulating amidase activity. Here, we investigated the function of amidases and LytM proteins in the opportunistic pathogen P seudomonas aeruginosa . In agreement with studies in other organisms, Pa AmiB and three LytM proteins were found to play crucial roles in P . aeruginosa cell separation, envelope integrity and antibiotic resistance. Importantly, the phenotype of amidase‐defective P . aeruginosa cells also differed in informative ways from the E . coli paradigm; Pa AmiB was found to be essential for viability and the successful completion of cell constriction. Our results thus reveal a key role for amidase activity in cytokinetic ring contraction. Furthermore, we show that the essential function of Pa AmiB can be bypassed in mutants activated for a C px‐like envelope stress response, suggesting that this signaling system may elicit the repair of division machinery defects in addition to general envelope damage.