Aarhus University Seal / Aarhus Universitets segl

An unusual topological structure of the HIV-1 Rev response element

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Xianyang Fang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, United States
  • Jinbu Wang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, United States
  • Ina P O'Carroll, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Michelle Mitchell, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Xiaobing Zuo, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, United States
  • Yi Wang, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Ping Yu, Structual Bipphysics Laboratory, SAIC-Frederick, United States
  • Yu Liu, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, United States
  • Jason W Rausch, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Marzena A Dyba, Structual Bipphysics Laboratory, SAIC-Frederick, United States
  • Jørgen Kjems
  • Charles D Schwieters, Division of Computational Bioscience, Center for Inforamtional Technology, National Institutes of Health, United States
  • Soenke Seifert, X-ray Science Divsion, Argonne National Laborarory, United States
  • Randall E Winans, X-ray Science Divsion, Argonne National Laborarory, United States
  • Norman R Watts, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, United States
  • Stephen J Stahl, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, United States
  • Paul T Wingfield, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, United States
  • R Andrew Byrd, Macromolecular NMR Section, Structural Biophysics Laboratory, Cente for Cancer Research, United States
  • Stuart F J Le Grice, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Alan Rein, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, United States
  • Yun-Xing Wang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, United States
Nuclear export of unspliced and singly spliced viral mRNA is a critical step in the HIV life cycle. The structural basis by which the virus selects its own mRNA among more abundant host cellular RNAs for export has been a mystery for more than 25 years. Here, we describe an unusual topological structure that the virus uses to recognize its own mRNA. The viral Rev response element (RRE) adopts an "A"-like structure in which the two legs constitute two tracks of binding sites for the viral Rev protein and position the two primary known Rev-binding sites ~55 Å apart, matching the distance between the two RNA-binding motifs in the Rev dimer. Both the legs of the "A" and the separation between them are required for optimal RRE function. This structure accounts for the specificity of Rev for the RRE and thus the specific recognition of the viral RNA.
Original languageEnglish
JournalCell
Volume155
Issue3
Pages (from-to)594-605
Number of pages12
ISSN0092-8674
DOIs
Publication statusPublished - 24 Oct 2013

    Research areas

  • Active Transport, Cell Nucleus, Base Sequence, Binding Sites, Cell Nucleus, HEK293 Cells, HIV-1, Humans, Molecular Sequence Data, Nuclear Pore, Nucleic Acid Conformation, RNA Folding, RNA, Messenger, RNA, Viral, Scattering, Small Angle, X-Ray Diffraction, rev Gene Products, Human Immunodeficiency Virus

See relations at Aarhus University Citationformats

ID: 68858798