PMID- 10438626
OWN - NLM
STAT- MEDLINE
DCOM- 19990924
LR  - 20061115
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 291
IP  - 2
DP  - 1999 Aug 13
TI  - Heteroduplex formation by human Rad51 protein: effects of DNA end-structure,
      hRP-A and hRad52.
PG  - 363-74
AB  - Purified human Rad51 protein (hRad51) catalyses ATP-dependent homologous pairing 
      and strand transfer reactions, characteristic of a central role in homologous
      recombination and double-strand break repair. Using single-stranded circular and 
      partially homologous linear duplex DNA, we found that the length of heteroduplex 
      DNA formed by hRad51 was limited to approximately 1.3 kb, significantly less than
      that observed with Escherichia coli RecA and Saccharomyces cerevisiae Rad51
      protein. Joint molecule formation required the presence of a 3' or 5'-overhang on
      the duplex DNA substrate and initiated preferentially at the 5'-end of the
      complementaryx strand. These results are consistent with a preference for strand 
      transfer in the 3'-5' direction relative to the single-stranded DNA. The human
      single-strand DNA-binding protein, hRP-A, stimulated hRad51-mediated joint
      molecule formation by removing secondary structures from single-stranded DNA, a
      role similar to that played by E. coli single-strand DNA-binding protein in
      RecA-mediated strand exchange reactions. Indeed, E. coli single-strand
      DNA-binding protein could substitute for hRP-A in hRad51-mediated reactions.
      Joint molecule formation by hRad51 was stimulated or inhibited by hRad52,
      dependent upon the reaction conditions. The inhibitory effect could be overcome
      by the presence of hRP-A or excess heterologous DNA.
CI  - Copyright 1999 Academic Press.
FAU - Baumann, P
AU  - Baumann P
AD  - Clare Hall Laboratories, Imperial Cancer Research Fund, South Mimms,
      Hertfordshire, EN6 3LD, UK.
FAU - West, S C
AU  - West SC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (DNA, Single-Stranded)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nucleic Acid Heteroduplexes)
RN  - 0 (RPA1 protein, human)
RN  - 0 (Replication Protein A)
RN  - EC 2.7.7.- (RAD51 protein, human)
RN  - EC 2.7.7.- (Rad51 Recombinase)
SB  - IM
MH  - DNA Repair
MH  - DNA, Single-Stranded/chemistry/*metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Humans
MH  - Nucleic Acid Conformation
MH  - *Nucleic Acid Heteroduplexes
MH  - Rad51 Recombinase
MH  - Replication Protein A
MH  - Structure-Activity Relationship
EDAT- 1999/08/10 00:00
MHDA- 1999/08/10 00:01
CRDT- 1999/08/10 00:00
PHST- 1999/08/10 00:00 [pubmed]
PHST- 1999/08/10 00:01 [medline]
PHST- 1999/08/10 00:00 [entrez]
AID - 10.1006/jmbi.1999.2954 [doi]
AID - S0022-2836(99)92954-6 [pii]
PST - ppublish
SO  - J Mol Biol. 1999 Aug 13;291(2):363-74. doi: 10.1006/jmbi.1999.2954.