Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P51532 (transcriptional activator)
 6,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To investigate the mechanisms of transcriptional regulation of Drosophila heat shock genes we studied the activity of a heat shock promoter in vitro after reconstitution into chromatin. Increasing the duration of nucleosome assembly progressively inactivated a plasmid template when it was transcribed with extracts of either unshocked or heat-shocked Drosophila embryos, despite induction of the transcriptional activator heat shock factor. Addition of the general transcription factor IID (TFIID) before nucleosome assembly did not significantly relieve nucleosomal inhibition, but TFIID potentiated the promoter to be responsive to activation by heat shock factor in the heat shock transcription extract. The potentiation by TFIID could be related to the nucleosome-free, hypersensitive state of heat shock promoters previously observed in vivo before heat shock induction and may be necessitated by the need to expedite activation of heat shock genes in response to environmental stress.
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PMID:Heat shock-regulated transcription in vitro from a reconstituted chromatin template. 203 56

Histone proteins have long been recognized as important regulators of eukaryotic gene expression. Condensation of DNA into chromatin by the core (H2A, H2B, H3, H4) and linker (H1, H5) histones effectively represses transcription initiation from the promoters of genes that have been packaged. Recently, eukaryotic transcriptional activators and coactivators (both positive and negative) resembling core and linker histone proteins have been discovered. Substantial progress has been made on structural and mechanistic studies of histones and histone-like transcription factors. Three-dimensional structures solved include the core histone octamer, an archael histone homodimer, two core histone-like subunits of transcription factor IID, a linker histone, and a linker histone-like transcriptional activator.
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PMID:Histone-like transcription factors in eukaryotes. 903 65

The bovine and human papillomavirus (BPV/HPV) E2 proteins bind specifically to palindromic sequences ACCGN4CGGT that are concentrated within the viral long control region, where they regulate viral oncogene transcription. E2 can activate viral promoters over relatively large distances within the viral genome and was shown to cooperate with a number of cellular transcription factors. Transcriptional activator proteins, such as E2, are thought to act, at least in part, by influencing the assembly and/or stability of preinitiation complexes and it has been suggested that the transcription factor IID, composed by the TATA-binding protein (TBP) and numerous TBP-associated factors (TAFs), is a possible target of this important viral protein. In this paper, we demonstrate that E2 proteins associate in vitro with several TAFs, in particular with TAFII250 and TAFII80. In addition, we observed that the association of TAFII250 with BPV1 E2 is stronger than with HPV18 E2 and that the carboxy terminal domain of both viral proteins is involved in this interaction. On the other hand, TAFII80 binds with similar strength to both E2 proteins through their amino terminal region. These observations may help to explain the different behavior of bovine and human E2 proteins, since BPV E2 is a stronger transcriptional activator than HPV18 E2.
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PMID:Specific in vitro interaction between papillomavirus E2 proteins and TBP-associated factors. 1556 46