Nucleic Acids Research Advance Access originally published online on January 30, 2007
Nucleic Acids Research 2007 35(4):1119-1133; doi:10.1093/nar/gkl1162
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1119-1133
© 2007 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.
Molecular Biology |
Meiotic association between Spo11 regulated by Rec102, Rec104 and Rec114
1Genetic System Regulation Laboratory, RIKEN Discovery Research Institute, Hirosawa 2-1, Wako, Saitama 351-0198, Japan, 2The Graduate School of Science and Engineering, Saitama University, Sakuraku, Saitama, Saitama 338-8570, Japan, 3Institut Curie, Centre de recherche, CNRS UMR7147, Université Piere et Marie Curie, 26 rue d’Ulm 75248, Paris Cedex 05, France and 4Shibata Distinguished Scientist Laboratory, RIKEN Discovery Research Institute, Hirosawa 2-1, Wako, Saitama 351-0198, Japan
*To whom correspondence should be addressed. Tel: +81 48 467 9277; Fax: +81 48 462 4691; Email: kohta{at}postman.riken.go.jp
Received November 10, 2006. Revised December 7, 2006. Accepted December 20, 2006.
Meiotic recombination is initiated by DNA double-stranded break (DSB) formation catalyzed by Spo11, a type-II topoisomerase-like transesterificase, presumably via a dimerization-mediated mechanism. We demonstrate the existence of in vivo interactions between Spo11 proteins carrying distinct tags, and the chromatin-binding and DSB activity of tagged Spo11 at innate and targeted DSB sites upon fusion to the Gal4 DNA-binding domain. First we identified the interaction between Spo11-3FLAG and Gal4BD-Spo11 proteins, and established that this interaction specifically occurs at the time of DSB formation. We then observed that presence of the Gal4BD-spo11Y135F (nuclease-deficient) protein allows Spo11-3FLAG recruitment at the GAL2 locus, indicative of the formation of a hetero-complex near the GAL2 UAS sites, but no formation of double- or single-strand breaks. Spo11 self-interaction around the GAL2 DSB site depends on other proteins for DSB formation, in particular Rec102, Rec104 and Rec114. Together, these results suggest that in vivo self-association of Spo11 during meiosis is genetically regulated. The results are discussed in relation to possible roles of Spo11 self-interaction in the control of the cleavage activity.
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