The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
HIV-1 Tat Assembles a Multifunctional Transcription Elongation Complex and Stably Associates with the 7SK snRNP
Open accessAbstract
SUMMARY HIV-1 transactivator Tat has greatly contributed to our understanding of transcription elongation by RNAPII. We purified HIV-1 Tat-associated factors from HeLa nuclear extract and show that Tat forms two distinct and stable complexes. Tatcom1 consists of the core active P-TEFb, MLL-fusion partners involved in leukemia (AF9, AFF4, AFF1, ENL, and ELL), and PAF1 complex. Importantly, Tatcom1 formation relies on P-TEFb while optimal CDK9 CTD-kinase activity is AF9 dependent. MLL-fusion partners and PAF1 are required for Tat transactivation. Tatcom2 is composed of CDK9, CycT1, and 7SK snRNP lacking HEXIM. Tat remodels 7SK snRNP by interacting directly with 7SK RNA, leading to the formation of a stress-resistant 7SK snRNP particle. Besides the identification of factors required for Tat transactivation and important for P-TEFb function, our data show a coordinated control of RNAPII elongation by different classes of transcription elongation factors associated in a single complex and acting at the same promoter.
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Cites
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Recruitment of P-TEFb for Stimulation of Transcriptional Elongation by the Bromodomain Protein Brd4
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7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
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Self-citationShilatifard, A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-134100 · Cited by 1,091
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Siliciano, R. F., & Greene, W. C. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a007096 · Cited by 513
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Metadata
- Authors
- Sobhian, B., Laguette, N., Yatim, A., Nakamura, M., Levy, Y., Kiernan, R., & Benkirane, M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 38
- Issue
- 3
- Pages
- 439-451
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2014017310
- Cited by
- 381
- References
- 48
- FWCI
- 14.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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