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Nucleic Acids Research Advance Access originally published online on July 25, 2008
Nucleic Acids Research 2008 36(15):5013-5020; doi:10.1093/nar/gkn471
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Nucleic Acids Research, 2008, Vol. 36, No. 15 5013-5020
© 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.


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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]


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