Structural rearrangements on HIV‐1 Tat (32–72) TAR complex formation

FEBS Letters

Kraft, Margot¹  Frank, Rainer W¹  Rösch, Paul²  Volkmann, Andrea²  Willbold, Dieter²  Schindler, Thomas³  Metzger, Armin U²  Steegborn, Clemens² 

[1] Zentrum für Molekularbiologie Heidelberg (ZMBH), D-69120 Heidelberg, Germany;Lehrstuhl für Biopolymere, Universität Bayreuth, D-95440 Bayreuth, Germany;Lehrstuhl für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

关键词: (HIV-1);    Tat-TAR interaction;    Fourier transform infrared spectroscopy;    Circular dichroism;    UV melting;    BIV;    bovine immunodeficiency virus;    BP1;    peptide fragment 32–72 comprising the core and basic sequence regions of HIV-1 Tat protein;    CD;    circular dichroism;    EIAV;    equine infectious anemia virus;    FTIR;    Fourier transform infrared;    HIV;    human immunodeficiency virus;    HPLC;    high-performance liquid chromatography;    MALDI;    matrix assisted laser desorption ionisation;    Tat;    trans-activator;    TAR;    trans-activation response element;   

DOI  :  10.1016/0014-5793(96)00314-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Expression of the early genes of the human immunodeficiency virus type-1 (HIV-1) genome is under the control of a trans-activator (Tat) protein. HIV-1 Tat action requires binding to TAR (trans-activation responsive element), an RNA sequence located at the 5′-end of all lentiviral mRNAs. We used various spectroscopic methods to investigate conformational changes on HIV-1 TAR binding to the HIV-1 (32–72) Tat peptide BP1. It comprises the RNA binding region and binds specifically to TAR. We conclude from our experiments that the regular A-form of the TAR RNA is slightly distorted towards the B-form when bound to BP1. Thus, the major groove is widened and the binding of BP1 facilitated. BP1 presumably adopts an extended conformation when binding to TAR and may fit well into the TAR major groove.

【 授权许可】

Unknown