Deletion of PBP1a/LpoA complex compromises cell envelope integrity in Shewanella oneidensis. Issue 12 (17th May 2018)

• Record Type: Journal Article
• Authors: Yin, Jianhua; Cai, Jingxiao; Yuan, Zhe; Wang, Zhewei; Gao, Haichun; Qiu, Juanping; Yu, Zhiliang
• Is Part Of: FEMS microbiology letters. Volume 365:Issue 12(2018:Jun.)
• Publication Date: 2018-05-17
• Subjects: Shewanella oneidensis -- penicillin-binding protein -- outer membrane lipoprotein -- peptidoglycan -- envelope integrity -- outer membrane permeability; Microbiology -- Periodicals; 579
• DOI: 10.1093/femsle/fny128
• Languages: English
• ISSNs: 0378-1097

Abstract

Abstract: High molecular weight penicillin-binding proteins (PBPs) are responsible for the biosynthesis of peptidoglycan. In Escherichia coli, PBP1a and PBP1b form multienzyme peptidoglycan-synthesizing complexes with outer membrane lipoproteins LpoA and LpoB, respectively. The two complexes appear to be largely redundant, although their distinct physiological roles remain unclear. PBP1a/LpoA and PBP1b/LpoB also exist in Shewanella oneidensis strain MR-1, but effects of the two complexes on aerobic growth and β-lactam resistance are quite different. In this study, the phenotypes of strains lacking a certain complex in S. oneidensis were compared. Deletion of PBP1a/LpoA caused aberrant cell morphology (including branches and bulges), enhanced sensitivity to various envelope stresses and outer membrane permeability. On the contrary, strains lacking PBP1b/LpoB displayed phenotypes similar to the wild type. Abstract : Deletion of PBP1a/LpoA, but not PBP1b/LpoB, affects cell envelope integrity in Shewanella oneidensis .