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

DOI: 10.1016/j.molcel.2021.06.025 DOI Help

Authors: Adam S. B. Jalal (John Innes Centre) , Ngat T. Tran (John Innes Centre) , Ling J. Wu (Newcastle University) , Karunakaran Ramakrishnan (John Innes Centre) , Martin Rejzek (John Innes Centre) , Giulia Gobbato (John Innes Centre) , Clare E. M. Stevenson (John Innes Centre) , David M. Lawson (John Innes Centre) , Jeff Errington (Newcastle University) , Tung B. K. Le (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Cell , VOL 34

State: Published (Approved)
Published: July 2021
Diamond Proposal Number(s): 18565 , 25108

Open Access Open Access

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.

Journal Keywords: nucleoid occlusion protein; Noc; ParB; CTP; membrane-binding protein; bacterial cell division; X-ray crystallography; in vitro reconstitution

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 20/07/2021 14:51

Documents:
1-s2.0-S1097276521005050-main.pdf

Discipline Tags:

Life Sciences & Biotech Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)