ArticleProceedings of the National Academy of Sciences of the United States of America2009
Tat acetylation modulates assembly of a viral-host RNA-protein transcription complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- The HIV-1 Transcriptional Program: From Initiation to Elongation Control.Journal of molecular biology · 2025Review
- The cell biology of HIV-1 latency and rebound.Retrovirology · 2024Review
- Review
- Article
- The Effect of miRNA Gene Regulation on HIV Disease.Frontiers in genetics · 2022Review
- The diverse roles of miRNAs in HIV pathogenesis: Current understanding and future perspectives.Frontiers in immunology · 2022Review
- Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019Review
- Cellular RelB interacts with the transactivator Tat and enhance HIV-1 expression.Retrovirology · 2018Article
- Article
- SHMT2 and the BRCC36/BRISC deubiquitinase regulate HIV-1 Tat K63-ubiquitylation and destruction by autophagy.PLoS pathogens · 2018Article
- Post-translational Modification-Based Regulation of HIV Replication.Frontiers in microbiology · 2018Review
- PJA2 ubiquitinates the HIV-1 Tat protein with atypical chain linkages to activate viral transcription.Scientific reports · 2017Article
- miRNA profiling of human naive CD4 T cells links miR-34c-5p to cell activation and HIV replication.The EMBO journal · 2017Article
- Role of Host Factors on the Regulation of Tat-Mediated HIV-1 Transcription.Current pharmaceutical design · 2017Review
- The new (dis)order in RNA regulation.Cell communication and signaling : CCS · 2016Review
- The 57th amino acid conveys the differential subcellular localization of human immunodeficiency virus-1 Tat derived from subtype B and C.Virus genes · 2016Article
- DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection.Proteomics · 2015Article
- Interaction of drugs of abuse and microRNA with HIV: a brief review.Frontiers in microbiology · 2015Review
- Manipulation of the host protein acetylation network by human immunodeficiency virus type 1.Critical reviews in biochemistry and molecular biology · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
HIV-1 Tat enhances viral transcription elongation by forming a ribonucleoprotein complex with transactivating responsive (TAR) RNA and P-TEFb, an elongation factor composed of cyclin T1 (CycT1) and Cdk9 that phosphorylates the C-terminal domain of RNA polymerase II. Previous studies have shown that Lys-28 in the activation domain (AD) of Tat is essential for HIV-1 transcription and replication and is acetylated by p300/CBP-associated factor (PCAF), but the mechanistic basis of the Lys-28 requirement is unknown. Here, we show that Lys-28 acetylation modulates the affinity and stability of HIV-1 Tat-CycT1-TAR complexes by enhancing an interaction with the CycT1 Tat-TAR recognition motif. High-affinity assembly correlates strongly with stimulation of transcription elongation in vitro and Tat activation in vivo. In marked contrast, bovine lentiviral Tat proteins have evolved a high-affinity TAR interaction that does not require PCAF-mediated acetylation of the Tat AD or CycT1 for RNA binding, whereas HIV-2 Tat has evolved an intermediate mechanism that uses a duplicated TAR element and CycT1 to enhance RNA affinity and consequently transcription activation. The coevolution of Tat acetylation, CycT1 dependence, and TAR binding affinity is seen in viral replication assays using Tat proteins that rely on CycT1 for TAR binding but are acetylation deficient, where compensatory mutations rapidly accrue in TAR to generate high-affinity, CycT1-independent complexes reminiscent of the bovine viruses. Thus, lysine acetylation can be used to modulate and evolve the strength of a viral-host RNA-protein complex, thereby tuning the levels of transcription elongation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.