Poly(A)(+) mRNA-binding protein Tudor-SN regulates stress granules aggregation dynamics

Xingjie Gao; Xue Fu; Juan Song; Yi Zhang; Xiaoteng Cui; Chao Su; Lin Ge; Jie Shao; Lingbiao Xin; Juha Saarikettu; Mei Mei; Xi Yang; Minxin Wei; Olli Silvennoinen; Zhi Yao; Jinyan He; Jie Yang

doi:10.1111/febs.13186

Poly(A)(+) mRNA-binding protein Tudor-SN regulates stress granules aggregation dynamics

FEBS J. 2015 Mar;282(5):874-90. doi: 10.1111/febs.13186. Epub 2015 Jan 26.

Authors

Xingjie Gao¹, Xue Fu, Juan Song, Yi Zhang, Xiaoteng Cui, Chao Su, Lin Ge, Jie Shao, Lingbiao Xin, Juha Saarikettu, Mei Mei, Xi Yang, Minxin Wei, Olli Silvennoinen, Zhi Yao, Jinyan He, Jie Yang

Affiliation

¹ Department of Biochemistry and Molecular Biology, Department of Immunology, School of Basic Medical Sciences, Tianjin Medical University, China; Laboratory of Molecular Immunology, Research Center of Basic Medical Science, Tianjin Medical University, China; Tianjin Key Laboratory of Cellular and Molecular Immunology, Tianjin Medical University, China; Key Laboratory of Educational Ministry of China, Tianjin Medical University, China.

PMID: 25559396
DOI: 10.1111/febs.13186

Abstract

Stress granules (SGs) and processing bodies (PBs) 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.

Keywords: PABP1; Tudor-SN; poly(A)+ mRNA; processing bodies; stress granules.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Argonaute Proteins / metabolism
Carrier Proteins / genetics
Carrier Proteins / metabolism
Cell Nucleus / metabolism
Cytoplasmic Granules / metabolism*
Cytosol / metabolism
DNA Helicases
Endonucleases
Endoribonucleases / metabolism
Eukaryotic Initiation Factors / metabolism
HeLa Cells
Humans
Insulin-Like Growth Factor Binding Protein 2 / genetics
Insulin-Like Growth Factor Binding Protein 2 / metabolism
Nuclear Proteins / genetics
Nuclear Proteins / metabolism*
Oxidative Stress
Poly A / metabolism
Poly(A)-Binding Protein I / metabolism
Poly-ADP-Ribose Binding Proteins
Polyribosomes / metabolism
Protein Interaction Maps
RNA Helicases
RNA Recognition Motif Proteins
RNA, Messenger / metabolism*
Recombinant Fusion Proteins / genetics
Recombinant Fusion Proteins / metabolism
Stress, Physiological
Trans-Activators / metabolism

Substances

AGO1 protein, human
Argonaute Proteins
Carrier Proteins
Eukaryotic Initiation Factors
IGFBP2 protein, human
Insulin-Like Growth Factor Binding Protein 2
Nuclear Proteins
Poly(A)-Binding Protein I
Poly-ADP-Ribose Binding Proteins
RNA Recognition Motif Proteins
RNA, Messenger
Recombinant Fusion Proteins
Trans-Activators
Poly A
Endonucleases
Endoribonucleases
SND1 protein, human
DCP1A protein, human
DCP2 protein, human
DNA Helicases
G3BP1 protein, human
RNA Helicases