English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/174334
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

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

AuthorsMartín-García, Bárbara; Martín-González, Alejandro; Carrasco,Carolina; Ruíz-Quero, Rubén; Díaz-Orejas, Ramón ; Aicart-Ramos,Clara; Moreno-Herrero, Fernando; Oliva, María A.; Hernández-Arriaga, A.M.
Issue DateJun-2018
PublisherOxford University Press
CitationNucleic Acids Research 46 (11): 5704-5716 (2018)
AbstractIn 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.
Publisher version (URL)http://dx.doi.org/ 10.1093/nar/gky370.
URIhttp://hdl.handle.net/10261/174334
DOI10.1093/nar/gky370
ISSN0305-1048
E-ISSN1362-4962
Appears in Collections:(CNB) Artículos
Files in This Item:
File Description SizeFormat 
The TubR-centromere complex adopts....pdfArtículo principal4,64 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.