SGS1 - A EUKARYOTIC HOMOLOG OF ESCHERICHIA-COLI RECQ THAT INTERACTS WITH TOPOISOMERASE-II IN-VIVO AND IS REQUIRED FOR FAITHFUL CHROMOSOME SEGREGATION

被引：379

作者：

WATT, PM ^{[1
]}

LOUIS, EJ ^{[1
]}

BORTS, RH ^{[1
]}

HICKSON, ID ^{[1
]}

机构：

[1] UNIV OXFORD, JOHN RADCLIFFE HOSP, INST MOLEC MED, YEAST GENET GRP, OXFORD OX3 9DU, ENGLAND

来源：

CELL | 1995年 / 81卷 / 02期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/0092-8674(95)90335-6

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：

Topoisomerase II (topo II) catalyzes the decatenation of interlinked DNA molecules and is essential for chromosome segregation. To test the hypothesis that the noncatalytic C-terminal domain of topo II is necessary for mediating interactions with other proteins required for chromosome segregation, we used a two-hybrid cloning strategy to identify proteins that interact with S. cerevisiae topo II in vivo. One protein identified (Sgs1p) is structurally related to E. coli RecQ protein and contains helicase signature! motifs. Strains lacking Sgs1p exhibit elevated levels of chromosome missegregation during both mitotic and meiotic division. We propose a model to account for the interaction of a topoisomerase and a helicase in the faithful segregation of newly replicated eukaryotic chromosomes.

引用

页码：253 / 260

页数：8

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