Human Rad50/Mre11 is a flexible complex that can tether DNA ends

被引:384
作者
de Jager, M
van Noort, J
van Gent, DC
Dekker, C
Kanaar, R
Wyman, C
机构
[1] Erasmus Univ, Dept Cell Biol & Genet, NL-3000 DR Rotterdam, Netherlands
[2] Delft Univ Technol, Dept Appl Phys, NL-2628 CJ Delft, Netherlands
[3] Delft Univ Technol, DIMES, NL-2628 CJ Delft, Netherlands
[4] Univ Rotterdam Hosp, Dept Radiat Oncol, Rotterdam, Netherlands
关键词
D O I
10.1016/S1097-2765(01)00381-1
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 human Rad50 protein, classified as a structural maintenance of chromosomes (SMC) family member, is complexed with Mre11 (R/M) and has important functions in at least two distinct double-strand break repair pathways. To find out what the common function of R/M in these pathways might be, we investigated its architecture. Scanning force microscopy showed that the complex architecture is distinct from the described SMC family members. R/M consisted of two highly flexible intramolecular coiled coils emanating from a central globular DNA binding domain. DNA end-bound R/M oligomers could tether linear DNA molecules. These observations suggest that a unified role for R/M in multiple aspects of DNA repair and chromosome metabolism is to provide a flexible, possibly dynamic, link between DNA ends.
引用
收藏
页码:1129 / 1135
页数:7
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