A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis in <i>Escherichia coli</i>

S Sohee Park (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University) W Wook-Jong Jeon (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University) Y Yeseul Lee (Department of Biotechnology, The Catholic University of Korea) C Chae Lim Lim (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University) E Eunyeong Lee (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University) H Han Byeol Oh (Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University) G Gyu Sung Lee (Department of Biopharmaceutical Convergence) O Oh Hyun Kwon (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University) B Bumhan Ryu (Research Solution Center, Institute for Basic Science) Y Yong-Joon Cho (Department of Molecular Bioscience, Kangwon National University) C Chung Sub Kim (Department of Biopharmaceutical Convergence) S Sung-il Yoon (Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University) J Jeong Min Chung (Department of Biotechnology, The Catholic University of Korea) H Hongbaek Cho (Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University)

Abstract

Bacterial cell wall assembly and remodeling require activities of peptidoglycan (PG) hydrolases as well as PG synthases. In particular, the activity of DD-endopeptidases, which cleave the 4-3 peptide crosslinks in PG, is essential for PG expansion in gram-negative bacteria. Maintaining optimal levels of DD-endopeptidases is critical for expanding PG without compromising its integrity. In Escherichia coli , the levels of major DD-endopeptidases, MepS and MepH, along with the lytic transglycosylase MltD, are controlled by the periplasmic protease Prc and its outer membrane adaptor NlpI. However, the mechanisms regulating the turnover of these PG hydrolases have remained unclear. In this study, we identified a periplasmic protein, BipP (formerly YhjJ), that negatively controls the NlpI-Prc system. Further analyses indicate that BipP exerts this control by interacting with NlpI and inhibiting its substrate recognition in response to low DD-endopeptidase activity, providing insight into the homeostatic control of PG hydrolysis and cell wall expansion.

Article Details

Volume / Issue Vol. 122, Issue 4
Published January 28, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (14)

S

Sohee Park

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University

W

Wook-Jong Jeon

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University

Y

Yeseul Lee

Department of Biotechnology, The Catholic University of Korea

C

Chae Lim Lim

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University

E

Eunyeong Lee

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University

H

Han Byeol Oh

Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University

G

Gyu Sung Lee

Department of Biopharmaceutical Convergence

O

Oh Hyun Kwon

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University

B

Bumhan Ryu

Research Solution Center, Institute for Basic Science

Y

Yong-Joon Cho

Department of Molecular Bioscience, Kangwon National University

C

Chung Sub Kim

Department of Biopharmaceutical Convergence

S

Sung-il Yoon

Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University

J

Jeong Min Chung

Department of Biotechnology, The Catholic University of Korea

H

Hongbaek Cho

Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University