Advances in structural studies of recombination mediator proteins.
作者： S. Korolev
DOI: 10.1016/J.BPC.2016.12.001
关键词: DNA repair 、 Genetics 、 DNA damage 、 PALB2 、 Homologous recombination 、 Recombinase 、 Biology 、 Function (biology) 、 DNA 、 Computational biology 、 RAD52
摘要: Recombination mediator proteins (RMPs) are critical for genome integrity in all organisms. They include phage UvsY, prokaryotic RecF, -O, -R (RecFOR) and eukaryotic Rad52, Breast Cancer susceptibility 2 (BRCA2) Partner localizer of BRCA2 (PALB2) proteins. PALB2 tumor suppressors implicated cancer. RMPs regulate binding RecA-like recombinases to sites DNA damage initiate the most efficient non-mutagenic repair broken chromosome other deleterious lesions. Mechanistically, stimulate a single-stranded (ssDNA) hand-off from ssDNA (ssbs) such as gp32, SSB RPA, recombinases, activating only at time site event. This review summarizes structural studies their implications understanding mechanism function. Comparative analysis is complicated due convergent evolution. In contrast evolutionary conserved ssbs extremely diverse sequence structure. Structural particularly important cases reveal common features entire family specific regulatory mechanisms each member. All characterized by DNA-binding domains variable protein interaction motifs. The complexity corresponds ever-growing number metabolism events they participate under normal pathological conditions requires additional comprehensive structure-functional studies.
sci-hub.se 参考文章(149)
A.G. Murzin, OB(oligonucleotide/oligosaccharide binding)-fold : common structural and functional solution for non-homologous sequences The EMBO Journal. ,vol. 12, pp. 861- 867 ,(1993) , 10.1002/J.1460-2075.1993.TB05726.X
Sergey Korolev, ATP-Binding Cassette Properties of Recombination Mediator Protein RecF InTech. ,(2011) , 10.5772/21178
K Hashimoto, T Yonesaki, The characterization of a complex of three bacteriophage T4 recombination proteins, uvsX protein, uvsY protein, and gene 32 protein, on single-stranded DNA. Journal of Biological Chemistry. ,vol. 266, pp. 4883- 4888 ,(1991) , 10.1016/S0021-9258(19)67731-8
Michael M. Cox, Recombinational DNA Repair in Bacteria and the RecA Protein Progress in Nucleic Acid Research and Molecular Biology. ,vol. 63, pp. 311- 366 ,(1999) , 10.1016/S0079-6603(08)60726-6
Keiko Umezu, Richard D Kolodner, Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein. Journal of Biological Chemistry. ,vol. 269, pp. 30005- 30013 ,(1994) , 10.1016/S0021-9258(18)43981-6
Weixing Zhao, Sivaraja Vaithiyalingam, Joseph San Filippo, David G. Maranon, Judit Jimenez-Sainz, Gerald V. Fontenay, Youngho Kwon, Stanley G. Leung, Lucy Lu, Ryan B. Jensen, Walter J. Chazin, Claudia Wiese, Patrick Sung, Promotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry Molecular Cell. ,vol. 59, pp. 176- 187 ,(2015) , 10.1016/J.MOLCEL.2015.05.032
Charles E. Bell, Structure and mechanism of Escherichia coli RecA ATPase. Molecular Microbiology. ,vol. 58, pp. 358- 366 ,(2005) , 10.1111/J.1365-2958.2005.04876.X
S.W. Morrical, B.M. Alberts, The UvsY protein of bacteriophage T4 modulates recombination-dependent DNA synthesis in vitro. Journal of Biological Chemistry. ,vol. 265, pp. 15096- 15103 ,(1990) , 10.1016/S0021-9258(18)77228-1
Aimee H Marceau, Soon Bahng, Shawn C Massoni, Nicholas P George, Steven J Sandler, Kenneth J Marians, James L Keck, Structure of the SSB-DNA polymerase III interface and its role in DNA replication The EMBO Journal. ,vol. 30, pp. 4236- 4247 ,(2011) , 10.1038/EMBOJ.2011.305
Joseph P. Menetski, Stephen C. Kowalczykowski, Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors. Journal of Molecular Biology. ,vol. 181, pp. 281- 295 ,(1985) , 10.1016/0022-2836(85)90092-0