The TubR-centromere complex adopts a double-ring segrosome structure in Type III partition systems.

Nucleic Acids Research
Bárbara Martín-GarcíaMaría A Oliva

Abstract

In prokaryotes, the centromere is a specialized segment of DNA that promotes the assembly of the segrosome upon binding of the Centromere Binding Protein (CBP). The segrosome structure exposes a specific surface for the interaction of the CBP with the motor protein that mediates DNA movement during cell division. Additionally, the CBP usually controls the transcriptional regulation of the segregation system as a cell cycle checkpoint. Correct segrosome functioning is therefore indispensable for accurate DNA segregation. Here, we combine biochemical reconstruction and structural and biophysical analysis to bring light to the architecture of the segrosome complex in Type III partition systems. We present the particular features of the centromere site, tubC, of the model system encoded in Clostridium botulinum prophage c-st. We find that the split centromere site contains two different iterons involved in the binding and spreading of the CBP, TubR. The resulting nucleoprotein complex consists of a novel double-ring structure that covers part of the predicted promoter. Single molecule data provides a mechanism for the formation of the segrosome structure based on DNA bending and unwinding upon TubR binding.

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Citations

Jan 11, 2019·Nucleic Acids Research·Daniel J Rigden, Xosé M Fernández
Jun 13, 2019·EcoSal Plus·Jean-Yves Bouet, Barbara E Funnell
Jun 4, 2021·Microbiology Resource Announcements·Cedric WoudstraMiia Lindström

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Methods Mentioned

BETA
GTPase
atomic
electron microscopy
gel filtration
AFM
PCR
electrophoresis
footprinting

Software Mentioned

Quantity One
Clustal Omega
LabVIEW
Heteroanalysis
WSxM
phiSite
SEDFIT

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