Molecular views of recombination proteins and their control
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm1127.pdf
Reference139 articles.
1. Cox, M. M. Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu. Rev. Genet. 35, 53–82 (2001).
2. Ogawa, T., Yu, X., Shinohara, A. & Egelman, E. H. Similarity of the yeast Rad51 filament to the bacterial RecA filament. Science 259, 1896–1899 (1993). The similarity between E. coli RecA and yeast Rad51 was seen by electron microscopy and indicated that the nucleoprotein filament structure that is important for recombination in bacteria has been conserved throughout evolution.
3. Benson, F. E., Stasiak, A. & West, S. C. Purification and characterisation of the human RAD51 protein, an analogue of E. coli RecA. EMBO J. 13, 5764–5771 (1994).
4. Yu, X., Jacobs, S. A., West, S. C., Ogawa, T. & Egelman, E. H. Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc. Natl Acad. Sci. USA 98, 8419–8424 (2001).
5. Pellegrini, L. et al. Insights into DNA recombination from the structure of a RAD51–BRCA2 complex. Nature 420, 287–293 (2002). Describes the crystal structure of a RAD51–BRC fusion protein, and illustrates how the interaction with a BRC repeat might 'cap' RAD51 in the monomeric form and inhibit nucleoprotein-filament formation.
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