Human Tudor staphylococcal nuclease (Tudor-SN) protein modulates the kinetics of AGTR1-3′UTR granule formation |
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| Authors: | Xingjie Gao Xuebin Shi Xue Fu Lin Ge Yi Zhang Chao Su Xi Yang Olli Silvennoinen Zhi Yao Jinyan He Minxin Wei Jie Yang |
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| Institution: | 1. Department of Biochemistry and Molecular Biology, Department of Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China;2. Laboratory of Molecular Immunology, Research Center of Basic Medical Science, Tianjin Medical University, Tianjin 300070, China;3. Tianjin Key Laboratory of Cellular and Molecular Immunology, Tianjin Medical University, Tianjin 300070, China;4. Key Laboratory of Educational Ministry of China, Tianjin Medical University, Tianjin 300070, China;5. Department of Immunology, University of Manitoba, 471 Apotex Centre, 750 McDermot Avenue, Winnipeg R3E 0T5, Canada;6. Institute of Medical Technology, University of Tampere, Tampere University Hospital, Biokatu 8, FI-33014 Tampere, Finland;g Department of Cardiovascular Surgery, Tianjin Medical University General Hospital, Tianjin 300070, China |
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| Abstract: | Human Tudor staphylococcal nuclease (Tudor-SN) interacts with the G3BP protein and is recruited into stress granules (SGs), the main type of discrete RNA-containing cytoplasmic foci structure that is formed under stress conditions. Here, we further demonstrate that Tudor-SN binds and co-localizes with AGTR1-3′UTR (3′-untranslated region of angiotensin II receptor, type 1 mRNA) into SG. Tudor-SN plays an important role in the assembly of AGTR1-3′UTR granules. Moreover, endogenous Tudor-SN knockdown can decrease the recovery kinetics of AGTR1-3′UTR granules. Collectively, our data indicate that Tudor-SN modulates the kinetics of AGTR1-3′UTR granule formation, which provides an additional biological role of Tudor-SN in RNA metabolism during stress. |
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| Keywords: | Tudor-SN Stress granules AGTR1 3&prime UTR |
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