ArticleMolecular and cellular biology1999
Tat activates human immunodeficiency virus type 1 transcriptional elongation independent of TFIIH kinase.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 43 citations in OpenAlex.
- Review
- Tip110 protein binds to unphosphorylated RNA polymerase II and promotes its phosphorylation and HIV-1 long terminal repeat transcription.The Journal of biological chemistry · 2014Article
- Impact of Tat Genetic Variation on HIV-1 Disease.Advances in virology · 2012Article
- 9-Aminoacridine inhibition of HIV-1 Tat dependent transcription.Virology journal · 2009Article
- Full and partial genome-wide assembly and disassembly of the yeast transcription machinery in response to heat shock.Genes & development · 2006Article
- Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo.Molecular and cellular biology · 2006Article
- A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat.Genes & development · 2005Article
- Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription.Journal of virology · 2004Article
- The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Cdk7 is required for full activation of Drosophila heat shock genes and RNA polymerase II phosphorylation in vivo.Molecular and cellular biology · 2003Article
- CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for transcription in the C. elegans embryo.Genes & development · 2002Article
- Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation.Molecular and cellular biology · 2002Article
- Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences.Molecular and cellular biology · 2002Article
- CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA.Molecular and cellular biology · 2000Article
- Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription.Molecular and cellular biology · 2000Article
- P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II.Molecular and cellular biology · 2000Review
- Specific interaction of Tat with the human but not rodent P-TEFb complex mediates the species-specific Tat activation of HIV-1 transcription.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tat stimulates human immunodeficiency virus type 1 (HIV-1) transcriptional elongation by recruitment of the human transcription elongation factor P-TEFb, consisting of Cdk9 and cyclin T1, to the HIV-1 promoter via cooperative binding to the nascent HIV-1 transactivation response RNA element. The Cdk9 kinase activity has been shown to be essential for P-TEFb to hyperphosphorylate the carboxy-terminal domain (CTD) of RNA polymerase II and mediate Tat transactivation. Recent reports have shown that Tat can also interact with the multisubunit transcription factor TFIIH complex and increase the phosphorylation of CTD by the Cdk-activating kinase (CAK) complex associated with the core TFIIH. These observations have led to the proposal that TFIIH and P-TEFb may act sequentially and in a concerted manner to promote phosphorylation of CTD and increase polymerase processivity. Here, we show that under conditions in which a specific and efficient interaction between Tat and P-TEFb is observed, only a weak interaction between Tat and TFIIH that is independent of critical amino acid residues in the Tat transactivation domain can be detected. Furthermore, immunodepletion of CAK under high-salt conditions, which allow CAK to be dissociated from core-TFIIH, has no effect on either basal HIV-1 transcription or Tat activation of polymerase elongation in vitro. Therefore, unlike the P-TEFb kinase activity that is essential for Tat activation of HIV-1 transcriptional elongation, the CAK kinase associated with TFIIH appears to be dispensable for Tat function.
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