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Poly(A) + mRNA‐binding protein Tudor‐SN regulates stress granules aggregation dynamics
Author(s) -
Gao Xingjie,
Fu Xue,
Song Juan,
Zhang Yi,
Cui Xiaoteng,
Su Chao,
Ge Lin,
Shao Jie,
Xin Lingbiao,
Saarikettu Juha,
Mei Mei,
Yang Xi,
Wei Minxin,
Silvennoinen Olli,
Yao Zhi,
He Jinyan,
Yang Jie
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13186
Subject(s) - stress granule , p bodies , messenger rna , cytoplasm , rna binding protein , messenger rnp , microbiology and biotechnology , poly(a) binding protein , cytosol , gene knockdown , rna , chemistry , biology , biochemistry , enzyme , gene , translation (biology)
Stress granules ( SG s) and processing bodies ( PB s) comprise the main types of cytoplasmic RNA foci during stress. Our previous data indicate that knockdown of human Tudor staphylococcal nuclease (Tudor‐SN) affects the aggregation of SGs. However, the precise molecular mechanism has not been determined fully. In the present study, we demonstrate that Tudor‐SN binds and colocalizes with many core components of SGs, such as poly(A) + mRNA binding protein 1, T‐cell internal antigen‐1‐related protein and poly(A) + mRNA, and SG/PB sharing proteins Argonaute 1/2, but not PB core proteins, such as decapping enzyme 1 a/b, confirming that Tudor‐SN is an SG‐specific protein. We also demonstrate that the Tudor‐SN granule actively communicates with the nuclear and cytosolic pool under stress conditions. Tudor‐SN can regulate the aggregation dynamics of poly(A) + mRNA‐containing SGs and selectively stabilize the SG‐associated mRNA during cellular stress.