Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB

Author:

Kureisaite-Ciziene Danguole1,Varadajan Aravindan2,McLaughlin Stephen H.1,Glas Marjolein2,Montón Silva Alejandro3,Luirink Rosa2,Mueller Carolin2,den Blaauwen Tanneke3,Grossmann Tom N.2,Luirink Joen2,Löwe Jan1ORCID

Affiliation:

1. MRC Laboratory of Molecular Biology, Cambridge, United Kingdom

2. Amsterdam Institute of Molecules, Medicines and Systems, VU University, Amsterdam, The Netherlands

3. Bacterial Cell Biology and Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands

Abstract

In most bacteria and archaea, filaments of FtsZ protein organize cell division. FtsZ forms a ring structure at the division site and starts the recruitment of 10 to 20 downstream proteins that together form a multiprotein complex termed the divisome. The divisome is thought to facilitate many of the steps required to make two cells out of one. FtsQ and FtsB are part of the divisome, with FtsQ being a central hub, interacting with most of the other divisome components. Here we show for the first time in detail how FtsQ interacts with its downstream partner FtsB and show that mutations that disturb the interface between the two proteins effectively inhibit cell division.

Funder

RCUK | Medical Research Council

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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