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Proc. Natl. Acad. Sci. USA, January 22, 2025 | https://doi.org/10.1073/pnas.2418854122
A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis in Escherichia coli
Sohee Park 1, Wook-Jong Jeon 1, Yeseul Lee 2, Chae Lim Lim 1, Eunyeong Lee 1, Han Byeol Oh 3, Gyu Sung Lee 4, Oh Hyun Kwon 1, Bumhan Ryu 5, Yong-Joon Cho 6 7, Chung Sub Kim 4 8, Sung-Il Yoon 3, Jeong Min Chung 2, Hongbaek Cho 1 *
1Department of Biological Sciences, College of Natural Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.
2Department of Biotechnology, The Catholic University of Korea, Bucheon 14662, Republic of Korea.
3Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
4Department of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon 16419, Republic of Korea.
5Research Solution Center, Institute for Basic Science, Daejeon 34126, Republic of Korea.
6Department of Molecular Bioscience, Kangwon National University, Chuncheon 24341, Republic of Korea.
7Multidimensional Genomics Research Center, Kangwon National University, Chuncheon 24341, Republic of Korea.
8School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
2Department of Biotechnology, The Catholic University of Korea, Bucheon 14662, Republic of Korea.
3Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
4Department of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon 16419, Republic of Korea.
5Research Solution Center, Institute for Basic Science, Daejeon 34126, Republic of Korea.
6Department of Molecular Bioscience, Kangwon National University, Chuncheon 24341, Republic of Korea.
7Multidimensional Genomics Research Center, Kangwon National University, Chuncheon 24341, Republic of Korea.
8School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
*Corresponding author: correspondence to Hongbaek Cho
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.
논문정보
- Research article
- 2025년 01월 (BRIC 등록일 2025-02-03)
- 국내 연구진
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