HIV-1 Tat protein can transactivate a heterologous TATAA element independent of viral promoter sequences and the trans-activation response element

AIDS ◽  
1997 ◽  
Vol 11 (2) ◽  
pp. 139-146 ◽  
Author(s):  
Kenneth A. Roebuck ◽  
Mohammed F. Rabbi ◽  
Martin F. Kagnoff
Keyword(s):  
Tat Protein ◽  
Viral Promoter ◽  
Response Element ◽  
Promoter Sequences ◽  
Activation Response ◽  
Hiv 1

scholarly journals Role of the Trans-activation Response Element in Dimerization of HIV-1 RNA

2004 ◽  
Vol 279 (21) ◽  
pp. 22243-22249 ◽  
Author(s):  
Ebbe S. Andersen ◽  
Sonia Antoranz Contera ◽  
Bjarne Knudsen ◽  
Christian K. Damgaard ◽  
Flemming Besenbacher ◽  
...  
Keyword(s):  
Response Element ◽  
Activation Response ◽  
Hiv 1

scholarly journals APOBEC3G Inhibits HIV-1 RNA Elongation by Inactivating the Viral Trans-Activation Response Element

2014 ◽  
Vol 426 (15) ◽  
pp. 2840-2853 ◽  
Author(s):  
Roni Nowarski ◽  
Ponnandy Prabhu ◽  
Edan Kenig ◽  
Yoav Smith ◽  
Elena Britan-Rosich ◽  
...  
Keyword(s):  
Response Element ◽  
Activation Response ◽  
Hiv 1

scholarly journals In vitro Evaluation of Bis-3-chloropiperidines as RNA Modulators Targeting TAR and TAR-protein Interaction

2021 ◽  
Author(s):  
Alice Sosic ◽  
Giulia Olivato ◽  
Caterina Carraro ◽  
Richard Göttlich ◽  
Dan Fabris ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Chaperone Activity ◽  
Next Generation ◽  
Response Element ◽  
In Vitro Evaluation ◽  
Loop Domain ◽  
Activation Response ◽  
Hiv 1

After a long limbo, RNA has gained its credibility as a druggable target, fully earning its de-served role in the next-generation area of pharmaceutical R&D. We have recently probed the Trans-Activation Response element (TAR), a RNA stem–bulge–loop domain of the HIV-1 genome with bis-3-chloropiperidines (B-CePs), and revealed the compounds unique behavior in stabiliz-ing TAR structure, thus impairing in vitro the chaperone activity of the HIV-1 nucleocapsid (NC) protein. Seeking to elucidate the determinants of B-CePs inhibition, we have further characterized here their effects on the target TAR and its NC recognition, while developing quantitative analyti-cal approaches for the study of multicomponent RNA-based interactions.

scholarly journals The HIV-1 Tat protein recruits a ubiquitin ligase to reorganize the 7SK snRNP for transcriptional activation

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Tyler B Faust ◽  
Yang Li ◽  
Curtis W Bacon ◽  
Gwendolyn M Jang ◽  
Amit Weiss ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Ubiquitin Ligase ◽  
Transcriptional Activation ◽  
Transcriptional Activity ◽  
Kinase Inhibitor ◽  
Tat Protein ◽  
Viral Promoter ◽  
Rnap Ii ◽  
Elongation Control ◽  
Hiv 1

The HIV-1 Tat protein hijacks P-TEFb kinase to activate paused RNA polymerase II (RNAP II) at the viral promoter. Tat binds additional host factors, but it is unclear how they regulate RNAP II elongation. Here, we identify the cytoplasmic ubiquitin ligase UBE2O as critical for Tat transcriptional activity. Tat hijacks UBE2O to ubiquitinate the P-TEFb kinase inhibitor HEXIM1 of the 7SK snRNP, a fraction of which also resides in the cytoplasm bound to P-TEFb. HEXIM1 ubiquitination sequesters it in the cytoplasm and releases P-TEFb from the inhibitory 7SK complex. Free P-TEFb then becomes enriched in chromatin, a process that is also stimulated by treating cells with a CDK9 inhibitor. Finally, we demonstrate that UBE2O is critical for P-TEFb recruitment to the HIV-1 promoter. Together, the data support a unique model of elongation control where non-degradative ubiquitination of nuclear and cytoplasmic 7SK snRNP pools increases P-TEFb levels for transcriptional activation.

scholarly journals Exosomes Derived from HIV-1-infected Cells Contain Trans-activation Response Element RNA

2013 ◽  
Vol 288 (27) ◽  
pp. 20014-20033 ◽  
Author(s):  
Aarthi Narayanan ◽  
Sergey Iordanskiy ◽  
Ravi Das ◽  
Rachel Van Duyne ◽  
Steven Santos ◽  
...  
Keyword(s):  
Response Element ◽  
Infected Cells ◽  
Activation Response ◽  
Hiv 1

scholarly journals Human GLI-2 Is a Tat Activation Response Element-Independent Tat Cofactor

2001 ◽  
Vol 75 (5) ◽  
pp. 2314-2323 ◽  
Author(s):  
Catherine M. Browning ◽  
Michael J. Smith ◽  
Nina M. Clark ◽  
Brian R. Lane ◽  
Camilo Parada ◽  
...  
Keyword(s):  
Regulatory Proteins ◽  
Tata Box ◽  
Hiv Replication ◽  
Response Element ◽  
Cyclin T1 ◽  
Gli Proteins ◽  
Dna Binding Site ◽  
Immunodeficiency Virus ◽  
Activation Response ◽  
Hiv 1

ABSTRACT Zinc finger-containing GLI proteins are involved in the development of Caenorhabditis elegans, Xenopus, Drosophila, zebrafish, mice, and humans. In this study, we show that an isoform of human GLI-2 strongly synergizes with the Tat transactivating proteins of human immunodeficiency virus types 1 and 2 (HIV-1 and -2) and markedly stimulates viral replication. GLI-2 also synergizes with the previously described Tat cofactor cyclin T1 to stimulate Tat function. Surprisingly, GLI-2/Tat synergy is not dependent on either a typical GLI DNA binding site or an intact Tat activation response element but does require an intact TATA box. Thus, GLI-2/Tat synergy results from a mechanism of action which is novel both for a GLI protein and for a Tat cofactor. These findings link the GLI family of transcriptional and developmental regulatory proteins to Tat function and HIV replication.

scholarly journals Conformational Dynamics of the HIV-1 Trans-Activation Response Element RNA Hairpin Bound to a Lab-Evolved Peptide

2018 ◽  
Vol 114 (3) ◽  
pp. 337a
Author(s):  
Chapin E. Cavender ◽  
Ivan A. Belashov ◽  
Joseph E. Wedekind ◽  
David H. Mathews
Keyword(s):  
Conformational Dynamics ◽  
Response Element ◽  
Activation Response ◽  
Rna Hairpin ◽  
Hiv 1
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