TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 279, No. 29, Issue of July 16, pp. 30385–30394, 2004 © 2004 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. hXRCC2 Enhances ADP/ATP Processing and Strand Exchange by hRAD51* Received for publication, June 9, 2003, and in revised form, April 29, 2004 Published, JBC Papers in Press, May 2, 2004, DOI 10.1074/jbc.M306066200 Kang Sup Shim, Christoph Schmutte, Gregory Tombline, Christopher D. Heinen, and Richard Fishel‡ From the Genetics and Molecular Biology Program, Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107 pairing and strand exchange activity (9 –14), the function(s) of The assembly of bacterial RecA, and its human homo- log hRAD51, into an operational ADP/ATP-regulated the remaining human RecA/RAD51 homologs is unknown. DNA-protein (nucleoprotein) filament is essential for Homology between RecA/RAD51 family members is largely homologous recombination repair (HRR). Yet hRAD51 confined to the Walker A/B nucleotide binding domains (2, 7, lacks the coordinated ADP/ATP processing exhibited by 15). These peptide motifs allow a number of diverse proteins to RecA and is less efficient in HRR reactions in vitro.In coordinate the free energy of nucleotide triphosphate (NTP) this study, we demonstrate that 
TI - hXRCC2 Enhances ADP/ATP Processing and Strand Exchange by hRAD51
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m306066200
DA - 2004-07-01
UR - https://www.deepdyve.com/lp/unpaywall/hxrcc2-enhances-adp-atp-processing-and-strand-exchange-by-hrad51-DLo3HrqeWo
DP - DeepDyve
ER -