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

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  • 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, USA
  • 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, USA
  • Ina P O'Carroll, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • Michelle Mitchell, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • 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, USA
  • Yi Wang, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • Ping Yu, Structual Bipphysics Laboratory, SAIC-Frederick, USA
  • 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, USA
  • Jason W Rausch, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • Marzena A Dyba, Structual Bipphysics Laboratory, SAIC-Frederick, USA
  • Jørgen Kjems
  • Charles D Schwieters, Division of Computational Bioscience, Center for Inforamtional Technology, National Institutes of Health, USA
  • Soenke Seifert, X-ray Science Divsion, Argonne National Laborarory, USA
  • Randall E Winans, X-ray Science Divsion, Argonne National Laborarory, USA
  • Norman R Watts, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
  • Stephen J Stahl, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
  • Paul T Wingfield, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
  • R Andrew Byrd, Macromolecular NMR Section, Structural Biophysics Laboratory, Cente for Cancer Research, USA
  • Stuart F J Le Grice, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • Alan Rein, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
  • 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, USA
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.
OriginalsprogEngelsk
TidsskriftCell
Vol/bind155
Nummer3
Sider (fra-til)594-605
Antal sider12
ISSN0092-8674
DOI
StatusUdgivet - 24 okt. 2013

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