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Title: Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions

Journal Article · · Structure
 [1];  [1];  [1];  [1];  [2];  [1];  [1];  [1];  [1];  [3];  [4];  [1];  [1];  [1];  [1]
  1. Univ. of Science and Technology of China, Hefei (China). Hefei National Lab. for Physical Sciences at the Microscale and School of Life Sciences
  2. Chinese Academy of Sciences (CAS), Beijing (China). National Center for Protein Science Shanghai and Shanghai Inst. of Biological Sciences
  3. Chinese Academy of Sciences (CAS), Shanghai (China). National Center for Protein Science Shanghai and Shanghai Inst. of Biological Sciences; Chinese Academy of Sciences (CAS), Beijing (China). National Lab. of Biomacromolecules and Inst. of Biophysics
  4. Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS) and X-ray Science Division

CsdA has been proposed to be essential for the biogenesis of ribosome and gene regulation after cold shock. However, the structure of CsdA and the function of its long C-terminal regions are still unclear. For this study, we solved all of the domain structures of CsdA and found two previously uncharacterized auxiliary domains: a dimerization domain (DD) and an RNA-binding domain (RBD). Small-angle X-ray scattering experiments helped to track the conformational flexibilities of the helicase core domains and C-terminal regions. Biochemical assays revealed that DD is indispensable for stabilizing the CsdA dimeric structure. We also demonstrate for the first time that CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD could specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); Shanghai Synchrotron Radiation Facility (SSRF); Ministry of Science and Technology (MOST) (China); Chinese Academy of Sciences (CAS); National Natural Science Foundation of China (NSFC)
Grant/Contract Number:
AC02-06CH11357; 2016YFA0500700; XDB08010101; XDB08030302; 31400629; 31330018; 31270760
OSTI ID:
1432954
Journal Information:
Structure, Vol. 25, Issue 12; ISSN 0969-2126
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 17 works
Citation information provided by
Web of Science

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The (p)ppGpp-binding GTPase Era promotes rRNA processing and cold adaptation in Staphylococcus aureus journal August 2019
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