| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print February 11, 2002
Microbiology and Immunology, Kimmel Cancer Center, Philadelphia, PA 19107
Corresponding Author: rfishel{at}lac.jci.tju.edu
The prototypical bacterial RecA protein promotes recombination/repair by catalyzing strand exchange between homologous DNAs. While the mechanism of strand exchange remains enigmatic, ATP-induced cooperativity between RecA protomers is critical for its function. A human RecA homolog, hRAD51, facilitates eukaryotic recombination/repair, although its ability to hydrolyze ATP and/or promote strand exchange appears distinct from the bacterial RecA. We have quantitatively examined the hRAD51 ATPase . The catalytic efficiency (kcat/Km) of the hRAD51 ATPase was approximately 50-fold lower than the RecA ATPase. Altering the ratio of DNA : hRAD51 as well as including salts which stimulate DNA strand exchange (ammonium sulfate and spermidine) were found to affect the catalytic efficiency of hRAD51. The average site size of hRAD51 was determined to be ~3 nt (bp) for both ssDNA and dsDNA. Importantly, hRAD51 lacks the magnitude of ATP-induced cooperativity that is a hallmark of RecA. Together these results suggest that hRAD51 may be unable to coordinate ATP hydrolysis between neighboring protomers.
J. Biol. Chem, 10.1074/jbc.M109915200
Submitted on October 12, 2001
Revised on February 7, 2002
Accepted on February 10, 2002
Biochemical characterization of the human RAD51 Protein: I. ATP hydrolysis
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  J. Mine, L. Disseau, M. Takahashi, G. Cappello, M. Dutreix, and J.-L. Viovy Real-time measurements of the nucleation, growth and dissociation of single Rad51 DNA nucleoprotein filaments Nucleic Acids Res., December 18, 2007; 35(21): 7171 - 7187. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Yang, J. Chintapalli, L. Sodagum, S. Baskin, A. Malhotra, K. Reiss, and L. G. Meggs Activated IGF-1R inhibits hyperglycemia-induced DNA damage and promotes DNA repair by homologous recombination Am J Physiol Renal Physiol, November 1, 2005; 289(5): F1144 - F1152. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Ristic, M. Modesti, T. van der Heijden, J. van Noort, C. Dekker, R. Kanaar, and C. Wyman Human Rad51 filaments on double- and single-stranded DNA: correlating regular and irregular forms with recombination function Nucleic Acids Res., June 8, 2005; 33(10): 3292 - 3302. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Tato, S. Zunzunegui, F. de la Cruz, and E. Cabezon TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase PNAS, June 7, 2005; 102(23): 8156 - 8161. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Wu, X. Qian, Y. He, I. A. Moya, and Y. Luo Crystal Structure of an ATPase-active Form of Rad51 Homolog from Methanococcus voltae: INSIGHTS INTO POTASSIUM DEPENDENCE J. Biol. Chem., January 7, 2005; 280(1): 722 - 728. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. I. Shalguev, Y. V. Kil, L. V. Yurchenko, E. A. Namsaraev, and V. A. Lanzov Rad51 Protein from the Thermotolerant Yeast Pichia angusta as a Typical but Thermodependent Member of the Rad51 Family Eukaryot. Cell, December 1, 2004; 3(6): 1567 - 1573. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. S. Shim, C. Schmutte, G. Tombline, C. D. Heinen, and R. Fishel hXRCC2 Enhances ADP/ATP Processing and Strand Exchange by hRAD51 J. Biol. Chem., July 16, 2004; 279(29): 30385 - 30394. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Yokoyama, N. Sarai, W. Kagawa, R. Enomoto, T. Shibata, H. Kurumizaka, and S. Yokoyama Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex Nucleic Acids Res., May 11, 2004; 32(8): 2556 - 2565. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. L. Chambers, A. J. Smith, and N. J. Savery A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd Nucleic Acids Res., November 15, 2003; 31(22): 6409 - 6418. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Trojanek, T. Ho, L. Del Valle, M. Nowicki, J. Y. Wang, A. Lassak, F. Peruzzi, K. Khalili, T. Skorski, and K. Reiss Role of the Insulin-Like Growth Factor I/Insulin Receptor Substrate 1 Axis in Rad51 Trafficking and DNA Repair by Homologous Recombination Mol. Cell. Biol., November 1, 2003; 23(21): 7510 - 7524. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Guhan and K. Muniyappa Mycobacterium tuberculosis RecA intein, a LAGLIDADG homing endonuclease, displays Mn2+ and DNA-dependent ATPase activity Nucleic Acids Res., July 15, 2003; 31(14): 4184 - 4191. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I. L. Urbatsch, G. A. Tyndall, G. Tombline, and A. E. Senior P-glycoprotein Catalytic Mechanism: STUDIES OF THE ADP-VANADATE INHIBITED STATE J. Biol. Chem., June 13, 2003; 278(25): 23171 - 23179. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Tombline, K.-S. Shim, and R. Fishel Biochemical Characterization of the Human RAD51 Protein. II. ADENOSINE NUCLEOTIDE BINDING AND COMPETITION J. Biol. Chem., April 19, 2002; 277(17): 14426 - 14433. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Tombline, C. D. Heinen, K.-S. Shim, and R. Fishel Biochemical Characterization of the Human RAD51 Protein. III. MODULATION OF DNA BINDING BY ADENOSINE NUCLEOTIDES J. Biol. Chem., April 19, 2002; 277(17): 14434 - 14442. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
