Molecular dissection of interactions between Rad51 and members of the recombination-repair group

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO and C. BENDIXEN. Molecular dissection of interactions between Rad51 and members of the recombination-repair group (olecular dissection of interactions between Rad51 and members of the recombination-repair group). Molecular and Cellular Biology. 2001, vol. 21, No 3, p. 966-976. ISSN 0270-7306.

Basic information

• Original name: Molecular dissection of interactions between Rad51 and members of the recombination-repair group
• Authors: KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO and C. BENDIXEN.
• Edition: Molecular and Cellular Biology, 2001, 0270-7306.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: Genetics and molecular biology
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 9.836
• RIV identification code: RIV/00216224:14310/01:00002738
• Organization unit: Faculty of Science
• UT WoS: 000166353700026

Abstract

Recombination is important for the repair of DNA damage and for chromosome segregation during meiosis; it has also been shown to participate in the regulation of cell proliferation. In the yeast Saccharomyces cerevisiae, recombination requires products of the RAD52 epistasis group. The Rad51 protein associates with the Rad51, Rad52, Rad54, and Rad55 proteins to form a dynamic complex. We describe a new strategy to screen for mutations which cause specific disruption of the interaction between certain proteins in the complex, leaving other interactions intact. This approach defines distinct protein interaction domains and protein relationships within the Rad51 complex. Alignment of the mutations onto the constructed three-dimensional model of the Rad51 protein reveal possible partially overlapping interfaces for the Rad51-Rad52 and the Rad51-Rad54 interactions. Rad51-Rad55 and Rad51-Rad51 interactions are affected by the same spectrum of mutations, indicating similarity between the two modes of binding. Finally, the detection of a subset of mutations within Rad51 which disrupt the interaction with mutant Rad52 protein but activate the interaction with Rad54 suggests that dynamic changes within the Rad51 protein may contribute to an ordered reaction process.

Links

• ME 276, research and development project: Name: Racionální re-design mikrobiálních enzymů podílejících se na degradaci toxických organických polutantů

Investor: Ministry of Education, Youth and Sports of the CR, Rational re-design of microbial enzymes involved in degradation of toxic organic pollutants.

• MSM 143100005, plan (intention): Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism