2002
DOI: 10.1074/jbc.m109917200
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Biochemical Characterization of the Human RAD51 Protein

Abstract: Adenosine nucleotides affect the ability of RecA⅐single-stranded DNA (ssDNA) nucleoprotein filaments to cooperatively assume and maintain an extended structure that facilitates DNA pairing during recombination. Here we have determined that ADP and ATP/ATP␥S affect the DNA binding and aggregation properties of the human RecA homolog human RAD51 protein (hRAD51). These studies have revealed significant differences between hRAD51 and RecA. In the presence of ATP␥S, RecA forms a stable complex with ssDNA, while th… Show more

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Cited by 40 publications
(17 citation statements)
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References 49 publications
(59 reference statements)
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“…Moreover, ADP 3 ATP exchange appears to depend on the extent of ADP saturation. These and additional studies presented in the following paper hRAD51 Nucleotide Binding/Exchange (37) are consistent with the notion that elevated ADP induces an irreversible aggregate structure that may only be relevant to in vitro studies.…”
Section: Discussionsupporting
confidence: 67%
“…Moreover, ADP 3 ATP exchange appears to depend on the extent of ADP saturation. These and additional studies presented in the following paper hRAD51 Nucleotide Binding/Exchange (37) are consistent with the notion that elevated ADP induces an irreversible aggregate structure that may only be relevant to in vitro studies.…”
Section: Discussionsupporting
confidence: 67%
“…Unlike bacterial RecA protein, yeast or human Rad51 readily bind dsDNA [118, 153]. This biochemical property poses a significant problem for the cell, as Rad51 may form dead-end complexes on chromosomal DNA, which exists in vast excess over sites of DNA damage, where Rad51 is destined to assemble on ssDNA [117] (Fig.…”
Section: Functions Of Rad54 Proteinmentioning
confidence: 99%
“…Although hRad51 shares many structural and functional similarities with RecA and the general process of recombination is similar for both, it differs significantly from RecA in certain biochemical characteristics. RecA has a very strong preference for nucleation on ssDNA ( 4 , 5 , 17 ) and ATP hydrolysis promotes its dissociation from ssDNA and dsDNA ( 17–20 ), whereas hRad51 shows a preferential affinity for dsDNA ( 21 ), it has a very low ATPase activity ( 6 ) and ATP hydrolysis does not seem to correlate with hRad51 dissociation from dsDNA ( 22 , 23 ). Since efficient strand exchange requires preferential binding to ssDNA rather than dsDNA ( 7 , 17 ), this might explain hRad51's weaker strand-exchange activity in vitro when compared to RecA, and suggests that one of the roles of the numerous other proteins involved in HR in vivo may be to favour formation of hRad51–ssDNA nucleoprotein filaments over dsDNA ones.…”
Section: Introductionmentioning
confidence: 99%