Yeast Gis2 and its human ortholog CNBP are novel components of stress-induced RNP granules.
Yeast Gis2 and its human ortholog CNBP are novel components of stress-induced RNP granules.
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DOI：
10.1371/journal.pone.0052824
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Wolin SL
中科院分区：
文献类型：
--
作者：
Rojas M;Farr GW;Fernandez CF;Lauden L;McCormack JC;Wolin SL
Although a CCTG expansion in the gene encoding the zinc knuckle protein CNBP causes a common form of muscular dystrophy, the function of both human CNBP and its putative budding yeast ortholog Gis2 remain poorly understood. Here we report the protein interactions of Gis2 and the subcellular locations of both Gis2 and CNBP. We found that Gis2 exhibits RNA-dependent interactions with two proteins involved in mRNA recognition, the poly(A) binding protein and the translation initiation factor eIF4G. We show that Gis2 is a component of two large RNA-protein granules, processing bodies and stress granules, which contain translationally repressed mRNAs. Consistent with a functional ortholog, CNBP also associates with the poly(A) binding protein and accumulates in stress granules during arsenite treatment of human cells. These results implicate both Gis2 and CNBP in mRNA handling during stress.
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通讯作者：
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