Fragments of the HIV-1 Tat protein specifically bind TAR RNA

Science ◽  
1990 ◽  
Vol 249 (4974) ◽  
pp. 1281-1285 ◽  
Author(s):  
K. Weeks ◽  
C Ampe ◽  
S. Schultz ◽  
T. Steitz ◽  
D. Crothers
Keyword(s):  
Tat Protein ◽  
Tar Rna ◽  
Hiv 1

scholarly journals TAR-RNA binding by HIV-1 Tat protein is selectively inhibited by its L-enantiomer

1998 ◽  
Vol 26 (12) ◽  
pp. 2886-2890 ◽  
Author(s):  
A. Garbesi ◽  
F. Hamy ◽  
M. Maffini ◽  
G. Albrecht ◽  
T. Klimkait
Keyword(s):  
Rna Binding ◽  
Tat Protein ◽  
Tar Rna ◽  
Hiv 1

Mapping of HIV-1 Tat protein sequences required for binding to Tar RNA

Virology ◽  
1991 ◽  
Vol 182 (2) ◽  
pp. 570-577 ◽  
Author(s):  
James Kamine ◽  
Paul Loewenstein ◽  
Maurice Green
Keyword(s):  
Protein Sequences ◽  
Tat Protein ◽  
Tar Rna ◽  
Hiv 1

scholarly journals Rotational symmetry in ribonucleotide strand requirements for binding of HIV-1 Tat protein to TAR RNA

1993 ◽  
Vol 21 (1) ◽  
pp. 151-154 ◽  
Author(s):  
Richard W. Barnett ◽  
Ulrike Delling ◽  
Raya Kuperman ◽  
Nahum Sonenberg ◽  
Martin Sumner-Smith
Keyword(s):  
Rotational Symmetry ◽  
Tat Protein ◽  
Tar Rna ◽  
Hiv 1

scholarly journals Simultaneous recognition of HIV-1 TAR RNA bulge and loop sequences by cyclic peptide mimics of Tat protein

2009 ◽  
Vol 106 (29) ◽  
pp. 11931-11936 ◽  
Author(s):  
A. Davidson ◽  
T. C. Leeper ◽  
Z. Athanassiou ◽  
K. Patora-Komisarska ◽  
J. Karn ◽  
...  
Keyword(s):  
Cyclic Peptide ◽  
Tat Protein ◽  
Peptide Mimics ◽  
Tar Rna ◽  
Hiv 1

scholarly journals A functional genetic approach suggests a novel interaction between the human immunodeficiency virus type 1 (HIV-1) Tat protein and HIV-1 TAR RNA in vivo

2003 ◽  
Vol 84 (3) ◽  
pp. 603-606 ◽  
Author(s):  
Lars H. Lund ◽  
Britta Wahren ◽  
Mariano A. Garcia-Blanco
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Tat Protein ◽  
Cyclin T1 ◽  
Immunodeficiency Virus ◽  
Tar Rna ◽  
Hiv 1

Human immunodeficiency virus type 1 (HIV-1) Tat and human Cyclin T1 form a complex and together recognize the viral TAR RNA element with specificity. Using HIV-1/equine infectious anaemia virus TAR chimeras, we show that in addition to the well-characterized interaction with the bulge, Tat recognizes the distal stem and the loop of TAR. These data support previously proposed, but unproven, molecular models.

The N-terminus of HIV-1 Tat protein is essential for Tat-TAR RNA interaction

2005 ◽  
Vol 62 (3) ◽  
pp. 355-361 ◽  
Author(s):  
O. Chaloin ◽  
J. -C. Peter ◽  
J. -P. Briand ◽  
B. Masquida ◽  
C. Desgranges ◽  
...  
Keyword(s):  
Tat Protein ◽  
N Terminus ◽  
Tar Rna ◽  
Rna Interaction ◽  
Hiv 1

scholarly journals Targeting Tat-TAR RNA Interaction for HIV-1 Inhibition

2021 ◽  
Author(s):  
Awadh Alanazi ◽  
Andrey Ivanov ◽  
Namita Kumari ◽  
Xionghao Lin ◽  
Songping Wang ◽  
...  
Keyword(s):  
Selective Inhibition ◽  
Host Factors ◽  
Tat Protein ◽  
Toxic Compounds ◽  
Cyclin T1 ◽  
Inhibitory Compounds ◽  
Tar Rna ◽  
Rna Interaction ◽  
Anti Hiv ◽  
Hiv 1

HIV-1 Tat protein interacts with TAR RNA and recruits CDK9/cyclin T1 and other host factors to induce HIV-1 transcription. Thus Tat-TAR RNA interaction, which is unique for HIV-1, represents an attractive target for anti-HIV-1 therapeutics. To target Tat-TAR RNA interaction, we used a crystal structure of TAR RNA with acetylpromazine bound to the bulge of TAR RNA, to dock compounds from Enamine database containing 1.6 million individual compounds. Docking identified 173 compounds that were analyzed for the inhibition of HIV-1 infection. Top ten inhibitory compounds with IC50 ≤ 6 µM were selected and the three least toxic compounds, T6780107 (IC50=2.97 μM), T0516-4834 (IC50=0.2 μM) and T5628834 (IC50=3.46 μM), were further tested for HIV-1 transcription inhibition. Only T0516-4834 compound showed selective inhibition of Tat-induced HIV-1 transcription, whereas T6780107 compound inhibited equally basal and Tat-induced transcription and T5628834 compound only inhibited basal HIV-1 transcription. The T0516-4834 compound also showed strongest inhibition of HIV-1 gag RNA expression and p24 production in CEM T cells infected with HIV-1 IIIB. Of the three compounds, only the T0516-4834 compound disrupted Tat-TAR RNA interaction indicating that it might target TAR RNA. Also, of the three tested compounds, T5628834 but not T6780107 or T0516-4834 disrupted Tat-CDK9/cyclin T1 interaction. Taken together, our study identified novel compound T0516-4834 that disrupted Tat-TAR RNA interaction and inhibited Tat-induced transcription and HIV-1 infection suggesting that this compound might serve as a new lead for anti-HIV-1 therapeutics.

Refolded HIV-1 tat protein protects both bulge and loop nucleotides in TAR RNA from ribonucleolytic cleavage

Biochemistry ◽  
1991 ◽  
Vol 30 (32) ◽  
pp. 8060-8066 ◽  
Author(s):  
J. Wade Harper ◽  
Naomi J. Logsdon
Keyword(s):  
Tat Protein ◽  
Tar Rna ◽  
Hiv 1
Sign in / Sign up

Export Citation Format

Share Document