CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc.
Mol Cell
; 81(17): 3623-3636.e6, 2021 09 02.
Article
em En
| MEDLINE
| ID: mdl-34270916
ABSTRACT
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.
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MEDLINE
Assunto principal:
Pirofosfatases
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Bacillus subtilis
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Citidina Trifosfato
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article