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

Lookup NU author(s): Dr Ling Juan WuORCiD, Professor Jeff Errington FRSORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© 2021 The Author(s). 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.

Publication metadata

Author(s): Jalal ASB, Tran NT, Wu LJ, Ramakrishnan K, Rejzek M, Gobbato G, Stevenson CEM, Lawson DM, Errington J, Le TBK

Publication type: Article

Publication status: Published

Journal: Molecular Cell

Year: 2021

Volume: 81

Issue: 17

Pages: 3623-3636.e6

Print publication date: 02/09/2021

Online publication date: 15/07/2021

Acceptance date: 18/06/2021

Date deposited: 15/09/2021

ISSN (print): 1097-2765

ISSN (electronic): 1097-4164

Publisher: Cell Press

URL: https://doi.org/10.1016/j.molcel.2021.06.025

DOI: 10.1016/j.molcel.2021.06.025

PubMed id: 34270916

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