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- Publisher Website: 10.1002/j.1460-2075.1995.tb07006.x
- Scopus: eid_2-s2.0-0028859150
- PMID: 7835343
- WOS: WOS:A1995QD39900014
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Article: Novel mechanism and factor for regulation by HIV-1 Tat
Title | Novel mechanism and factor for regulation by HIV-1 Tat |
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Authors | |
Keywords | HIV Polymerase processivity Tat Tat-specific cellular factor Transcriptional activation |
Issue Date | 1995 |
Citation | EMBO Journal, 1995, v. 14, n. 2, p. 321-328 How to Cite? |
Abstract | Tat regulation of human immunodeficiency virus (HIV) transcription is unique because of its specificity for an RNA target, TAR, and its ability to increase the efficiency of elongation by polymerase. A reconstituted reaction that is Tat-specific and TAR-dependent for activation of HIV transcription has been used to identify and partially purify a cellular activity that is required for trans-activation by Tat, but not by other activators. In the reaction, Tat stimulates the efficiency of elongation by polymerase, whereas Sp1 and other DNA sequence-specific transcription factors activate the rate of initiation. Furthermore, while TATA binding protein (TBP)-associated factors (TAFs) in the TFIID complex are required for activation by transcription factors, they are dispensable for Tat function. Thus, Tat acts through a novel mechanism, which is mediated by a specific host cellular factor, to stimulate HIV-1 gene expression. |
Persistent Identifier | http://hdl.handle.net/10722/324987 |
ISSN | 2023 Impact Factor: 9.4 2023 SCImago Journal Rankings: 5.489 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Zhou, Qiang | - |
dc.contributor.author | Sharp, Phillip A. | - |
dc.date.accessioned | 2023-02-27T07:28:46Z | - |
dc.date.available | 2023-02-27T07:28:46Z | - |
dc.date.issued | 1995 | - |
dc.identifier.citation | EMBO Journal, 1995, v. 14, n. 2, p. 321-328 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.uri | http://hdl.handle.net/10722/324987 | - |
dc.description.abstract | Tat regulation of human immunodeficiency virus (HIV) transcription is unique because of its specificity for an RNA target, TAR, and its ability to increase the efficiency of elongation by polymerase. A reconstituted reaction that is Tat-specific and TAR-dependent for activation of HIV transcription has been used to identify and partially purify a cellular activity that is required for trans-activation by Tat, but not by other activators. In the reaction, Tat stimulates the efficiency of elongation by polymerase, whereas Sp1 and other DNA sequence-specific transcription factors activate the rate of initiation. Furthermore, while TATA binding protein (TBP)-associated factors (TAFs) in the TFIID complex are required for activation by transcription factors, they are dispensable for Tat function. Thus, Tat acts through a novel mechanism, which is mediated by a specific host cellular factor, to stimulate HIV-1 gene expression. | - |
dc.language | eng | - |
dc.relation.ispartof | EMBO Journal | - |
dc.subject | HIV | - |
dc.subject | Polymerase processivity | - |
dc.subject | Tat | - |
dc.subject | Tat-specific cellular factor | - |
dc.subject | Transcriptional activation | - |
dc.title | Novel mechanism and factor for regulation by HIV-1 Tat | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1002/j.1460-2075.1995.tb07006.x | - |
dc.identifier.pmid | 7835343 | - |
dc.identifier.scopus | eid_2-s2.0-0028859150 | - |
dc.identifier.volume | 14 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 321 | - |
dc.identifier.epage | 328 | - |
dc.identifier.isi | WOS:A1995QD39900014 | - |