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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Bibliographic Details
Published in:Molecular cell 2021-09, Vol.81 (17), p.3623-3636.e6
Main Authors: 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.
Format: Article
Language:English
Subjects:
bacterial cell division
CTP
in vitro reconstitution
membrane-binding protein
Noc
nucleoid occlusion protein
ParB
X-ray crystallography
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Summary: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. [Display omitted] •CTP is required for Noc to form a higher-order nucleoprotein complex on DNA•CTP binding switches DNA-entrapped Noc to a membrane-active state•CTP hydrolysis likely reverses the association between Noc-DNA and the membrane•The membrane-targeting helix adopts an autoinhibitory conformation in apo-Noc Jalal et al. report that the nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly regulated by CTP. CTP binding switches the Noc-DNA complex from a membrane-inactive state to an active state, thus ensuring productive recruitment of DNA to the bacterial cell membrane.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2021.06.025