SPOP is essential for DNA-protein cross-link repair in prostate cancer cells: SPOP-dependent removal of topoisomerase 2A from the topoisomerase 2A-DNA cleavage complex.
SPOP is essential for DNA-protein cross-link repair in prostate cancer cells: SPOP-dependent removal of topoisomerase 2A from the topoisomerase 2A-DNA cleavage complex.
复制标题
SPOP 对于前列腺癌细胞中 DNA-蛋白质交联修复至关重要:SPOP 依赖性地从拓扑异构酶 2A-DNA 裂解复合物中去除拓扑异构酶 2A。
DOI:
10.1091/mbc
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发表时间:
2020
影响因子:
3.3
通讯作者:
et al.
中科院分区:
文献类型:
--
作者:
Watanabe R; Kikugawa T;Saika T;Higashiyama S;et al.
TheChlamydomonasanterograde intraflagellar transport motor, kinesin-2, is isolated as a heterotrimeric complex containing two motor subunits and a nonmotor subunit known as kinesin-associated polypeptide or KAP. One of the two motor subunits is encoded by theFLA10gene. The sequence of the second motor subunit was obtained by mass spectrometry and sequencing. It shows 46.9% identity with the Fla10 motor subunit and the gene maps to linkage group XII/XIII near RPL9. The temperature-sensitive flagellar assembly mutantsfla1andfla8are linked to this kinesin-2 motor subunit. In each strain, a unique single point mutation gives rise to a unique single amino acid substitution within the motor domain. Thefla8strain is namedfla8-1and thefla1strain is namedfla8-2. Thefla8andfla10alleles show a chromosome loss phenotype. To analyze this chromosome loss phenotype, intragenic revertants offla8-1, fla8-2, andfla10-14were generated. The analysis of the mutants and the revertants demonstrates the importance of a pocket in the amino terminus of these motor subunits for both motor activity and for a novel, dominant effect on the fidelity of chromosome segregation.