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  Characterization of two highly similar Rad51 homologs of Physcomitrella patens

Ayora, S., Piruat, J. I., Luna, R., Reiss, B., Russo, V. E. A., Aguilera, A., et al. (2002). Characterization of two highly similar Rad51 homologs of Physcomitrella patens. Journal of Molecular Biology, 316(1), 35-49.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E14-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E15-C
Genre: Journal Article

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 Creators:
Ayora, S., Author
Piruat, J. I., Author
Luna, R., Author
Reiss, B.1, Author              
Russo, V. E. A., Author
Aguilera, A., Author
Alonso, J. C., Author
Affiliations:
1Dept. of Genetic Principles of Plant Breeding (Jozef Schell), MPI for Plant Breeding Research, Max Planck Society, ou_1113567              

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Free keywords: DNA recombination; DNA repair; RecA; ATPases; strand exchange
 Abstract: The moss Physcomitrella patens, which is a land plant with efficient homologous recombination, encodes two Rad51 proteins PpaRad51.1 and PpaRad51.2). The PpaRad51.1 and PpaRad51.2 proteins, which share 94% identity between them, interact with themselves and with each other. Both proteins bind ssDNA and dsDNA in a Mg2+ and pH-dependent manner, with a stoichiometry of similar toone PpaRad51.1 monomer per 3(+/-1) nt or bp and one PpaRad51.2 monomer per 1(+/-0.5) nt or bp, respectively. At neutral pH, a 1.6-fold excess of both proteins is required for ssDNA and dsDNA binding. PpaRad51.1 and PpaRad51.2 show ssDNA- dependent ATPase activity and efficiently promote strand annealing in a nucleotide-independent but in a Mg2+-depenclent manner. Both proteins promote joint-molecule formation, DNA strand invasion and are able to catalyse strand exchange in the presence of Mg2+ and ATP. No further increase in the activities is observed when both proteins are present in the same reaction. None of the PpaRad51 gene products complement the DNA repair and recombination phenotype of Saccharomyces cerevisiae rad51Delta mutants. However, PpaRad51.1 confers a dominant- negative DNA repair phenotype, and both PpaRad51 proteins reduce the levels of double-strand break-induced recombination when overexpressed in S. cerevisiae wt cells. These results suggest that both PpaRad51 proteins are bona fide Rad51 proteins that may contribute, in a different manner, to homologous recombination, and that they might replace ScRad51 in a hypothetical yeast protein complex inactivating different functions required for recombinational repair. (C) 2002 Elsevier Science Ltd.

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Language(s): eng - English
 Dates: 2002-02-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 127296
ISI: 000174025900004
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 316 (1) Sequence Number: - Start / End Page: 35 - 49 Identifier: ISSN: 0022-2836