NDLI: Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding.

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Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding.

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Single-molecule kinetics of the eukaryotic initiation factor 4AI upon RNA unwinding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sun, Yingjie Atas, Evrim Lindqvist, Lisa M. Sonenberg, Nahum Pelletier, Jerry Meller, Amit
Description	Country affiliation: United States Author Affiliation: Sun Y ( Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA.); Atas E ( Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA.); Lindqvist LM ( Department of Medical Biology, The University of Melbourne, Parkville, VIC 3010, Australia); Sonenberg N ( Department of Biochemistry and The Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, QC H3G 1Y6, Canada.); Pelletier J ( Department of Biochemistry and The Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, QC H3G 1Y6, Canada.); Meller A ( Department of Biomedical Engineering, Boston University, Boston, MA 02215, USA)
Abstract	The eukaryotic translation initiation factor 4AI (eIF4AI) is the prototypical DEAD-box RNA helicase. It has a 'dumbbell' structure consisting of two domains connected by a flexible linker. Previous studies demonstrated that eIF4AI, in conjunction with eIF4H, bind to loop structures and repetitively unwind RNA hairpins. Here, we probe the conformational dynamics of eIF4AI in real time using single-molecule FRET. We demonstrate that eIF4AI/eIF4H complex can repetitively unwind RNA hairpins by transitioning between an eIF4AI 'open' and a 'closed' conformation using the energy derived from ATP hydrolysis. Our experiments directly track the conformational changes in the catalytic cycle of eIF4AI and eIF4H, and this correlates precisely with the kinetics of RNA unwinding. Furthermore, we show that the small-molecule eIF4A inhibitor hippuristanol locks eIF4AI in the closed conformation, thus efficiently inhibiting RNA unwinding. These results indicate that the large conformational changes undertaken by eIF4A during the helicase catalytic cycle are rate limiting.
File Format	HTM / HTML
ISSN	09692126
Issue Number	7
Volume Number	22
e-ISSN	18784186
Journal	Structure
Language	English
Publisher	Elsevier
Publisher Date	2014-07-08
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Eukaryotic Initiation Factor-4a Chemistry Nucleic Acid Conformation Protein Conformation Rna Animals Base Sequence Dead-box Rna Helicases Genetics Metabolism Fluorescence Resonance Energy Transfer Humans Kinetics Models, Molecular Molecular Sequence Data Mutation Protein Binding Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
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3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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