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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]}

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: NATURE COMMUNICATIONS; v. 12, n. 1 MAY 20 2021.
• Citações Web of Science: 0

Resumo

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)

• Processo FAPESP: 17/12436-9 - ANTIBIO-BAC: a parede bacteriana como alvo para o desenvolvimento de novos agentes antimicrobianos
• Beneficiário: Andrea Dessen de Souza e Silva
• Modalidade de apoio: Auxílio à Pesquisa - Programa SPEC
• Processo FAPESP: 15/19906-5 - Identificação de novos agentes anti-bacterianos em bibliotecas de produtos naturais
• Beneficiário: Fernanda Rodrigues da Costa
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 11/52067-6 - Estruturação de complexos macromoleculares da parede bacteriana: biossíntese e virulência
• Beneficiário: Andrea Dessen de Souza e Silva
• Modalidade de apoio: Auxílio à Pesquisa - Programa SPEC
• Processo FAPESP: 18/07148-7 - Exploração da maquinaria de formação da parede celular bacteriana para o desenvolvimento de novos antibióticos
• Beneficiário: Fernanda Rodrigues da Costa
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Doutorado