Self-association of MreC as a regulatory signal in bacterial cell wall elongation

Author(s):Show less -

Martins, Alexandre ^[1] ; Contreras-Martel, Carlos ^[1] ; Janet-Maitre, Manon ^{[1, 2]} ; Miyachiro, Mayara M. ^[1] ; Estrozi, Leandro F. ^[1] ; Trindade, Daniel Maragno ^[3] ; Malospirito, Caique C. ^{[3, 4]} ; Rodrigues-Costa, Fernanda ^{[3, 4]} ; Imbert, Lionel ^[1] ; Job, Viviana ^{[1, 2]} ; Schoehn, Guy ^[1] ; Attree, Ina ^{[1, 2]} ; Dessen, Andrea ^{[3, 1]}

Affiliation

^[1] Univ Grenoble Alpes, Inst Biol Struct IBS, CNRS, CEA, Grenoble - France

^[2] Univ Grenoble Alpes, CNRS, ERL5261, CEA, IRIG, BCI, INSERM, UMR1036, Grenoble - France

^[3] CNPEM, Brazilian Biosci Natl Lab LNBio, Campinas, SP - Brazil

^[4] Univ Estadual Campinas, Inst Biol, Dept Genet Evolucao Microbiol & Imunol, UNICAMP, Campinas, SP - Brazil

• Document type: Journal article
• Source: NATURE COMMUNICATIONS; v. 12, n. 1 MAY 20 2021.
• Web of Science Citations: 0

Abstract

The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be dependent on MreC self-association. Here, we use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC from Pseudomonas aeruginosa in atomic detail. MreC monomers interact in head-to-tail fashion. Longitudinal and lateral interfaces are essential for oligomerization in vitro, and a phylogenetic analysis of proteobacterial MreC sequences indicates the prevalence of the identified interfaces. Our results are consistent with a model where MreC's ability to alternate between self-association and interaction with the cell wall biosynthesis machinery plays a key role in the regulation of elongasome activity. MreC is a membrane-associated protein that modulates the activity of the elongasome, a protein complex that controls cell wall formation in rod-shaped bacteria. Here, the authors use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC in atomic detail. (AU)

• FAPESP's process: 17/12436-9 - ANTIBIO-BAC: exploring the bacterial cell wall as a target for novel antibiotherapies
• Grantee: Andrea Dessen de Souza e Silva
• Support Opportunities: Research Projects - SPEC Program
• FAPESP's process: 15/19906-5 - Identification of new antibacterial agents in libraries of natural products
• Grantee: Fernanda Rodrigues da Costa
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 11/52067-6 - Assembly and structure of macromolecular complexes involved in bacterial cell wall: biosynthesis and virulence
• Grantee: Andrea Dessen de Souza e Silva
• Support Opportunities: Research Projects - SPEC Program
• FAPESP's process: 18/07148-7 - New antibiotic development through exploration of the bacterial cell wall formation machinery
• Grantee: Fernanda Rodrigues da Costa
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate