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CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc

ATP- and GTP-dependent molecular switches are extensively used to control functions of proteins in a wide range of biological processes. However, CTP switches are rarely reported. Here, we report that a nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly reg...

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Detalles Bibliográficos
Autores principales: Jalal, Adam S.B., Tran, Ngat T., Wu, Ling J., Ramakrishnan, Karunakaran, Rejzek, Martin, Gobbato, Giulia, Stevenson, Clare E.M., Lawson, David M., Errington, Jeff, Le, Tung B.K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8429893/
https://www.ncbi.nlm.nih.gov/pubmed/34270916
http://dx.doi.org/10.1016/j.molcel.2021.06.025
Descripción
Sumario:ATP- and GTP-dependent molecular switches are extensively used to control functions of proteins in a wide range of biological processes. However, CTP switches are rarely reported. Here, we report that a nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly regulated by a CTP switch. In Bacillus subtilis, Noc nucleates on 16 bp NBS sites before associating with neighboring non-specific DNA to form large membrane-associated nucleoprotein complexes to physically occlude assembly of the cell division machinery. By in vitro reconstitution, we show that (1) CTP is required for Noc to form the NBS-dependent nucleoprotein complex, and (2) CTP binding, but not hydrolysis, switches Noc to a membrane-active state. Overall, we suggest that CTP couples membrane-binding activity of Noc to nucleoprotein complex formation to ensure productive recruitment of DNA to the bacterial cell membrane for nucleoid occlusion activity.