Interaction of HIV Tat Peptides With tRNAPhe from Yeast

1998 ◽  
Vol 63 (6) ◽  
pp. 842-850 ◽  
Author(s):  
Iwona Buskiewicz ◽  
Malgorzata Giel-Pietraszuk ◽  
Piotr Mucha ◽  
Piotr Rekowski ◽  
Gotfryd Kupryszewski ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Tat Peptide ◽  
Phosphodiester Bond ◽  
Tat Peptides ◽  
Hiv Tat ◽  
Immunodeficiency Virus ◽  
Arginine Residues ◽  
Tar Rna ◽  
Rna Complex ◽  
Direct Recognition

We present data on the interaction of arginine-rich peptides of human immunodeficiency virus (HIV-Tat) with tRNAPhe of Saccharomyces cerevisiae. We have found that tRNA forms complexes with the Tat1 peptide of amino acid sequence GRKKRRQRRRA and its mutants where R is replaced by D-arginine, citrulline or ornithine. The structure of tRNA-Tat1 complex was probed by specific RNases digestions and Pb2+-induced cleavage of phosphodiester bond of guanosine. The nucleotide sequence UGGG located in the dihydrouridine loop of tRNAPhe binds to Tat peptide and therefore is specifically protected against RNases and is not hydrolyzed by Pb2+ ion. It seems that the peptide-RNA complex formation depends on direct recognition of guanine moieties of tRNA with arginine residues. These interactions are similar to those observed in many DNA-protein complexes, but are different from those previously observed for TAR RNA-Tat complexes.

scholarly journals Interaction of HIV Tat model peptides with tRNA and 5S rRNA.

1997 ◽  
Vol 44 (3) ◽  
pp. 591-600 ◽  
Author(s):  
M Giel-Pietraszuk ◽  
M Z Barciszewska ◽  
P Mucha ◽  
P Rekowski ◽  
G Kupryszewski ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Protein Complexes ◽  
5S Rrna ◽  
Lupinus Luteus ◽  
Rich Region ◽  
Rna Molecules ◽  
Hiv Tat ◽  
Immunodeficiency Virus ◽  
Arginine Residues ◽  
Tar Rna

New data are presented on the interaction of model synthetic peptides containing an arginine-rich region of human immunodeficiency virus (HIV-Tat), with native RNA molecules: tRNA(Phe) of Saccharomyces cerevisiae and 5S rRNA from Lupinus luteus. Both RNA species form complexes with the Tat1 (GRKKRRQRRRA) and Tat2 (GRKKRRQRRRAPQDSQTHQASLSKQPA) peptides, as shown by electrophoretic gel shift and RNase footprint assays, and CD measurements. The nucleotide sequence UGGG located in the dihydrouridine loop of tRNAPhe as well as in the loop D of 5S rRNA is specifically protected against RNases. Our data indicate direct interactions of guanine of RNA moieties with arginine residues. These interactions seem similar to those observed in DNA-protein complexes, but different from those previously observed in the TAR RNA-Tat complexes.

Tethering of proteins to RNAs using the bovine immunodeficiency virus–Tat peptide and BIV–TAR RNA

2012 ◽  
Vol 427 (2) ◽  
pp. 130-132 ◽  
Author(s):  
Motoaki Wakiyama ◽  
Yoko Kaitsu ◽  
Reiko Muramatsu ◽  
Koji Takimoto ◽  
Shigeyuki Yokoyama
Keyword(s):  
Bovine Immunodeficiency Virus ◽  
Tat Peptide ◽  
Immunodeficiency Virus ◽  
Tar Rna

Site-Specific Cross-Linking of Amino Acids in the Basic Region of Human Immunodeficiency Virus Type 1 Tat Peptide to Chemically Modified TAR RNA Duplexes

Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 3096-3108 ◽  
Author(s):  
Mark A. Farrow ◽  
Fareed Aboul-ela ◽  
David Owen ◽  
Alexander Karpeisky ◽  
Leonid Beigelman ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cross Linking ◽  
Tat Peptide ◽  
Site Specific ◽  
Chemically Modified ◽  
Immunodeficiency Virus ◽  
Rna Duplexes ◽  
Tar Rna ◽  
Basic Region

RNA AND N3′ → P5′ KISSING APTAMERS TARGETED TO THETRANS-ACTIVATION RESPONSIVE (TAR) RNA OF THE HUMAN IMMUNODEFICIENCY VIRUS-1

2001 ◽  
Vol 20 (4-7) ◽  
pp. 441-449 ◽  
Author(s):  
Fabien Darfeuille ◽  
Christian Cazenave ◽  
Sergei Gryaznov ◽  
Frédéric Ducongé ◽  
Carmelo Di Primo ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Immunodeficiency Virus ◽  
Tar Rna ◽  
Human Immunodeficiency Virus 1

scholarly journals Monocytes Treated with Human Immunodeficiency Virus Tat Kill Uninfected CD4+ Cells by a Tumor Necrosis Factor-Related Apoptosis-Induced Ligand-Mediated Mechanism

2003 ◽  
Vol 77 (12) ◽  
pp. 6700-6708 ◽  
Author(s):  
Yida Yang ◽  
Ilia Tikhonov ◽  
Tracy J. Ruckwardt ◽  
Mahmoud Djavani ◽  
Juan Carlos Zapata ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
T Cells ◽  
Cell Death ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Cell Surface Expression ◽  
Monocyte Subset ◽  
Hiv Tat ◽  
Immunodeficiency Virus ◽  
Necrosis Factor

ABSTRACT The human immunodeficiency virus (HIV) Tat protein has a critical role in viral transcription, but this study focuses on its additional role as an extracellular effector of lymphocyte cell death. It is well known that Tat induces tumor necrosis factor-related apoptosis-induced ligand (TRAIL) in peripheral blood mononuclear cells (PBMC), and we show that the majority of TRAIL is produced by the monocyte subset of PBMC. Human monocytes and U937 monoblastoid cells did not take up soluble HIV Tat-86, as T cells did, yet produced more TRAIL than did T cells. TRAIL secretion was induced by Tat and by a cysteine-rich peptide of Tat but not by sulfhydryl-modified Tat toxoid. Although there was only a slight increase in cell surface expression of TRAIL on monocytes, sufficient TRAIL was secreted to be toxic for T cells. The cytotoxicity of Tat-stimulated monocyte medium could be blocked by a TRAIL-neutralizing antibody. T cells treated with Tat did not secrete enough TRAIL to mediate cell death in our assay. Remarkably, uninfected T cells are more susceptible to TRAIL than are HIV-infected T cells. The production of TRAIL by Tat-stimulated monocytes provides a mechanism by which HIV infection can destroy uninfected bystander cells.

Antibodies against a multiple-peptide conjugate comprising chemically modified human immunodeficiency virus type-1 functional Tat peptides inhibit infection

Peptides ◽  
2007 ◽  
Vol 28 (3) ◽  
pp. 496-504 ◽  
Author(s):  
Krishnakumar Devadas ◽  
Robert A. Boykins ◽  
Indira K. Hewlett ◽  
Owen L. Wood ◽  
Kathleen A. Clouse ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Chemically Modified ◽  
Tat Peptides ◽  
Immunodeficiency Virus

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.

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