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

J 2001

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

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO, C. BENDIXEN et. al.

Základní údaje

Originální název

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

Autoři

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO a C. BENDIXEN

Vydání

Molecular and Cellular Biology, 2001, 0270-7306

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 9.836

Kód RIV

RIV/00216224:14310/01:00002738

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000166353700026

Změněno: 13. 2. 2002 06:02, prof. Mgr. Jiří Damborský, Dr.

Anotace

V originále

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.

Návaznosti

ME 276, projekt VaV

Název: Racionální re-design mikrobiálních enzymů podílejících se na degradaci toxických organických polutantů

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Racionální re-design mikrobiálních enzymů podílejících se na degradaci toxických organických polutantů

MSM 143100005, záměr

Název: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Citovat

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO a C. BENDIXEN. Molecular dissection of interactions between Rad51 and members of the recombination-repair group. Molecular and Cellular Biology. 2001, roč. 21, č. 3, s. 966-976. ISSN 0270-7306.

@article{346013,
   author = {Krejčí, Lumír and Damborský, Jiří and Thomsen, B. and Duno, M. and Bendixen, C.},
   article_number = {3},
   language = {eng},
   issn = {0270-7306},
   journal = {Molecular and Cellular Biology},
   title = {Molecular dissection of interactions between Rad51 and members of the recombination-repair group},
   volume = {21},
   year = {2001}
}

TY  - JOUR
ID  - 346013
AU  - Krejčí, Lumír - Damborský, Jiří - Thomsen, B. - Duno, M. - Bendixen, C.
PY  - 2001
TI  - Molecular dissection of interactions between Rad51 and members of the recombination-repair group
JF  - Molecular and Cellular Biology
VL  - 21
IS  - 3
SP  - 966
EP  - 966
SN  - 02707306
N2  - 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.
ER  -

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO a C. BENDIXEN. Molecular dissection of interactions between Rad51 and members of the recombination-repair group. \textit{Molecular and Cellular Biology}. 2001, roč.~21, č.~3, s.~966-976. ISSN~0270-7306.

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