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PapA , a peptidoglycan‐associated protein, interacts with OmpC and maintains cell envelope integrity
Author(s) -
Wang YunHao,
Chen HongHe,
Huang Zhou,
Li XiaoJing,
Zhou Nan,
Liu Chang,
Jiang ChengYing,
Li DeFeng,
Liu ShuangJiang
Publication year - 2021
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.15038
Subject(s) - peptidoglycan , cell envelope , biology , bacterial outer membrane , porin , mutant , bacterial cell structure , microbiology and biotechnology , membrane protein , periplasmic space , cell wall , biochemistry , bacteria , membrane , genetics , gene , escherichia coli
Summary The bacterial cell envelope is critical to support and maintain cellular life. In Gram‐negative bacterial cells, the outer membrane and the peptidoglycan layer are two important parts of the cell envelope and they harbour abundant proteins. Here, we report the identification and characterization of a previously unknown p eptidoglycan‐ a ssociated p rotein, PapA, from the Gram‐negative Comamonas testosteroni . PapA bound peptidoglycan with its C‐terminal domain and interacted with the outer‐membrane porin OmpC. The PapA‐OmpC complex riveted the outer membrane and the peptidoglycan layer, and played a role in maintaining cell envelope integrity. When papA was disrupted, the mutant CNB‐1Δ papA apparently had an outer membrane partly separated from the peptidoglycan layer. Phenotypically, the mutant CNB‐1Δ papA lost chemotactic responses and had longer lag‐phase of growth, less flagellation and higher sensitivity to harsh environments. Totally, 1093 functionally unknown PapA homologues were identified from the public NR protein database and they were mainly distributed in Burkholderiales of Betaproteobacteria. Our finding provides a clue that the PapA homologous proteins might function as a rivet to maintain cell envelope integrity in those Gram‐negative bacteria.