A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments

被引：83

作者：

Sheridan, Sean D. ^{[1
]}

Yu, Xiong ^{[2
]}

Roth, Robyn ^{[3
]}

Heuser, John E. ^{[3
]}

Sehorn, Michael G. ^{[4
]}

Sung, Patrick ^{[4
]}

Egelman, Edward H. ^{[2
]}

Bishop, Douglas K. ^{[1
,5
]}

机构：

[1] Univ Chicago, Comm Genet, Chicago, IL 60637 USA

[2] Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA

[3] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA

[4] Yale Univ, Sch Med, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[5] Univ Chicago, Dept Mol Genet & Cell Biol, Chicago, IL 60637 USA

来源：

NUCLEIC ACIDS RESEARCH | 2008年 / 36卷 / 12期

关键词：

D O I：

10.1093/nar/gkn352

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The eukaryotic RecA homologs Rad51 and Dmc1 are essential for strand exchange between homologous chromosomes during meiosis. All members of the RecA family of recombinases polymerize on DNA to form helical nucleoprotein filaments, which is the active form of the protein. Here we compare the filament structures of the Rad51 and Dmc1 proteins from both human and budding yeast. Previous studies of Dmc1 filaments suggested that they might be structurally distinct from filaments of other members of the RecA family, including Rad51. The data presented here indicate that Rad51 and Dmc1 filaments are essentially identical with respect to several structural parameters, including persistence length, helical pitch, filament diameter, DNA base pairs per helical turn and helical handedness. These data, together with previous studies demonstrating similar in vitro recombinase activity for Dmc1 and Rad51, support the view that differences in the meiotic function of Rad51 and Dmc1 are more likely to result from the influence of distinct sets of accessory proteins than from intrinsic differences in filament structure.

引用

页码：4057 / 4066

页数：10

共 58 条

[1] The N-terminal domain of the human Rad51 protein binds DNA: Structure and a DNA binding surface as revealed by NMR [J].