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This content will become publicly available on December 5, 2018

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

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.
Authors:
 [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
Publication Date:
Grant/Contract Number:
AC02-06CH11357; 2016YFA0500700; XDB08010101; XDB08030302; 31400629; 31330018; 31270760
Type:
Accepted Manuscript
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 25; Journal Issue: 12; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); Shanghai Synchrotron Radiation Facility (SSRF); Ministry of Science and Technology (MOST) (China); Chinese Academy of Sciences (CAS); National Natural Science Foundation of China (NNSFC)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; CsdA; DEAD-box helicase; crystal structure; small-angle X-ray scattering; dimerization domain; ATPase activity; unwinding activity; RNA binding
OSTI Identifier:
1432954