Skip Navigation



Nucleic Acids Research Advance Access published online on July 25, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn471
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (7248K) Freely available
Right arrow Screen PDF (730K) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
36/15/5013    most recent
gkn471v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Honda, M.
Right arrow Articles by Mikawa, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Honda, M.
Right arrow Articles by Mikawa, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

RecR forms a ring-like tetramer that encircles dsDNA by forming a complex with RecF

Masayoshi Honda1,2, Tetsuro Fujisawa3,4, Takehiko Shibata1,2 and Tsutomu Mikawa1,2,3,*

1RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, 2Internatnional Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, 3RIKEN SPring-8 center, 1-1-1 Kouto, Sayo, Hyogo 679-5148 and 4Department of Biomolecular Science, Graduate School of Engineering, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan

*To whom correspondence should be addressed. Tel: +81 45 508 7224; Fax: +81 405 508 7364; Email: mikawa{at}riken.jp

Received April 7, 2008. Revised July 5, 2008. Accepted July 7, 2008.

In the RecFOR pathway, the RecF and RecR proteins form a complex that binds to DNA and exerts multiple functions, including directing the loading of RecA onto single-stranded (ss) DNA regions near double-stranded (ds) DNA–ssDNA junctions and preventing it from forming a filament beyond the ssDNA region. However, neither the structure of the RecFR complex nor its DNA-binding mechanism was previously identified. Here, size-exclusion chromatography and small-angle X-ray scattering data indicate that Thermus thermophilus (tt) RecR binds to ttRecF to form a globular structure consisting of four ttRecR and two ttRecF monomers. In addition, a low resolution model shows a cavity in the central part of the complex, suggesting that ttRecR forms a ring-like tetramer inside the ttRecFR complex. Mutant ttRecR proteins lacking the N- or C-terminal interfaces that are required for tetramer formation are unable to form a complex with ttRecF. Furthermore, a ttRecFR complex containing the DNA-binding deficient ttRecR K23E/R27E double mutant, which contains mutations lying inside the ring, exhibits significantly reduced dsDNA binding. Thus, we propose that the ring-like ttRecR tetramer has a key role in tethering the ttRecFR complex onto dsDNA and that the ring structure may function as a clamp protein.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. Makharashvili, T. Mi, O. Koroleva, and S. Korolev
RecR-mediated Modulation of RecF Dimer Specificity for Single- and Double-stranded DNA
J. Biol. Chem., January 16, 2009; 284(3): 1425 - 1434.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.