参与染色体分离的Irr1/Scc3蛋白具有核质双重定位。
The Irr1/Scc3 protein implicated in chromosome segregation in has a dual nuclear-cytoplasmic localization.
作者信息
Kowalec Piotr, Fronk Jan, Kurlandzka Anna
机构信息
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, 02-106 Warsaw, Poland.
Department of Molecular Biology, Faculty of Biology, Institute of Biochemistry, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland.
出版信息
Cell Div. 2017 Jan 3;12:1. doi: 10.1186/s13008-016-0027-0. eCollection 2017.
BACKGROUND
Correct chromosome segregation depends on the sister chromatid cohesion complex. The essential, evolutionarily conserved regulatory protein Irr1/Scc3, is responsible for the complex loading onto DNA and for its removal. We found that, unexpectedly, Irr1 is present not only in the nucleus but also in the cytoplasm.
RESULTS
We show that Irr1 protein is enriched in the cytoplasm upon arrest of yeast cells in G1 phase following nitrogen starvation, diauxic shift or α-factor action, and also during normal cell cycle. Despite the presence of numerous Crm1-dependent export signals, the cytoplasmic pool of Irr1 is not derived through export from the nucleus but instead is simply retained in the cytoplasm. Cytoplasmic Irr1 interacts with the Imi1 protein implicated in glutathione homeostasis and mitochondrial integrity.
CONCLUSIONS
Besides regulation of the sister chromatid cohesion complex in the nucleus Irr1 appears to have an additional role in the cytoplasm, possibly through interaction with the cytoplasmic protein Imi1.
背景
正确的染色体分离依赖于姐妹染色单体黏连复合体。必需的、进化上保守的调节蛋白Irr1/Scc3负责该复合体加载到DNA上以及将其移除。我们意外地发现，Irr1不仅存在于细胞核中，也存在于细胞质中。
结果
我们发现，在氮饥饿、双相转变或α因子作用后酵母细胞在G1期停滞时，以及在正常细胞周期中，Irr1蛋白在细胞质中富集。尽管存在众多依赖Crm1的输出信号，但Irr1的细胞质池并非通过从细胞核输出而来，而是简单地保留在细胞质中。细胞质中的Irr1与参与谷胱甘肽稳态和线粒体完整性的Imi1蛋白相互作用。
结论
除了在细胞核中调节姐妹染色单体黏连复合体之外，Irr1似乎在细胞质中还有额外作用，可能是通过与细胞质蛋白Imi1相互作用实现的。
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