ArticleJournal of virology2002
The Tat protein of human immunodeficiency virus type 1 (HIV-1) can promote placement of tRNA primer onto viral RNA and suppress later DNA polymerization in HIV-1 reverse transcription.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- SLC38A9 is directly involved in Tat-induced endolysosome dysfunction and senescence in astrocytes.Life science alliance · 2025Article
- MultipleACS medicinal chemistry letters · 2020Article
- HIV, Tat and dopamine transmission.Neurobiology of disease · 2017Review
- A mutant tat protein inhibits HIV-1 reverse transcription by targeting the reverse transcription complex.Journal of virology · 2015Article
- Reverse Transcription of Retroviruses and LTR Retrotransposons.Microbiology spectrum · 2015Review
- Retrospective on the all-in-one retroviral nucleocapsid protein.Virus research · 2014Review
- Dynamic interactions of the HIV-1 Tat with nucleic acids are critical for Tat activity in reverse transcription.Nucleic acids research · 2014Article
- Article
- Comparative nucleic acid chaperone properties of the nucleocapsid protein NCp7 and Tat protein of HIV-1.Virus research · 2012Review
- HIV-1 reverse transcription.Cold Spring Harbor perspectives in medicine · 2012Review
- Challenges in understanding the immunopathogenesis of Cryptosporidium infections in humans.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2011Review
- The HIV-1 Tat protein has a versatile role in activating viral transcription.Journal of virology · 2011Article
- The RNA annealing mechanism of the HIV-1 Tat peptide: conversion of the RNA into an annealing-competent conformation.Nucleic acids research · 2011Article
- Comparative analysis of RNA/protein dynamics for the arginine-rich-binding motif and zinc-finger-binding motif proteins encoded by HIV-1.Biophysical journal · 2010Article
- Construction of a doxycycline-dependent simian immunodeficiency virus reveals a nontranscriptional function of tat in viral replication.Journal of virology · 2007Article
- Molecular mechanisms by which human immunodeficiency virus type 1 integrase stimulates the early steps of reverse transcription.Journal of virology · 2007Article
- Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription.Nucleic acids research · 2007Article
- Selection of TAR RNA-binding chameleon peptides by using a retroviral replication system.Journal of virology · 2004Article
- Human immunodeficiency virus type 1 protease regulation of tat activity is essential for efficient reverse transcription and replication.Journal of virology · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human immunodeficiency virus type-1 Tat has been proposed to play a role in the regulation of reverse transcription. We previously demonstrated that wild-type Tat can augment viral infectivity by suppressing the reverse transcriptase (RT) reaction at late stages of the viral life cycle in order to prevent the premature synthesis of potentially deleterious viral DNA products. Here we have performed a detailed analysis of the cell-free reverse transcription reaction to elucidate the mechanism(s) whereby Tat can affect this process. Our results show that Tat can suppress nonspecific DNA elongation while moderately affecting the specific initiation stage of reverse transcription. In addition, Tat has an RNA-annealing activity and can promote the placement of tRNA onto viral RNA. This points to a functional homology between Tat and the viral nucleocapsid (NC) protein that is known to be directly involved in this process. Experiments using a series of mutant Tat proteins revealed that the cysteine-rich and core domains of Tat are responsible for suppression of DNA elongation, while each of the cysteine-rich, core, and basic domains, as well as a glutamine-rich region in the C-terminal domain, are important for the placement of tRNA onto the viral RNA genome. These results suggest that Tat can play at least two different roles in the RT reaction, i.e., suppression of DNA polymerization and placement of tRNA onto viral RNA. We believe that the first of these activities of Tat may contribute to the overall efficiency of reverse transcription of the viral genome during a new round of infection as well as to enhanced production of infectious viral particles. We hypothesize that the second activity, illustrating functional homology between Tat and NC, suggests a potential role for NC in the displacement of Tat during viral maturation.
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