Transcriptional regulation by the immediate early protein of pseudorabies virus during in vitro nucleosome assembly

Workman, Jerry L.; Abmayr, Susan M.; Cromlish, Wanda; Roeder, Robert G.

doi:10.1016/0092-8674(88)90044-x

Cited by 181 publications

(101 citation statements)

References 53 publications

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“…In vitro assembled actin gene chromatin does not show any detectable transcriptional activity in the assembly reaction mixture (not shown). This is in agreement with the observation that the assembly process in vitro prevents efficient initiation of transcription [14]. As reported in [7] injected SV40 chromatin is converted by oocyte chromatin factors into an activated form.…”

Section: Resultssupporting

confidence: 93%

Transcriptional characteristics of in vitro assembled chromatin assayed by microinjection into Xenopus laevis oocytes

et al. 1989

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Plasmid DNA was in vitro assembled into chromatin using an S-150 extract of Xenopus laevis oocytes. By varying the assembly temperature and DNA concentration it is possible to generate fully or partially assembled molecules. The fate of the in vitro preassembled molecules injected into X. laevis oocyte nuclei and their transcriptional activity were studied.Completely reconstituted molecules underwent a rearrangement of their chromatin structure after injection and showed reduced transcriptional activity compared to protein-free DNA or partially reconstituted chromatin.

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Section: Resultssupporting

confidence: 93%

Transcriptional characteristics of in vitro assembled chromatin assayed by microinjection into Xenopus laevis oocytes

et al. 1989

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“…Consistent with this key role for TFIID, early studies of the mechanism of action of eukaryotic activators demonstrated physical and functional interactions with native TFIID that in turn facilitated preinitiation complex assembly and function (12,13,30). More recent studies have indicated that TFIID is a large multisubunit complex in both Drosophila (5,18) and human (1,2,25,26,33) cells, consisting of the TATA box-binding protein (TFIIDr or TBP) and a number of tightly associated subunits.…”

mentioning

confidence: 85%

Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit.

Kokubo¹,

Gong²,

Yamashita³

et al. 1993

Mol. Cell. Biol.

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Transcription initiation factor TFHD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. To further understand the role of the 85-kDa TFIID subunit (p85), we have cloned the corresponding cDNA with a probe based on an amino acid sequence of the purified protein. The recombinant p85 interacts directly with both the TATA box-binding subunit (TFIIDr or TBP) and the 110-kDa subunit (p110) of TFHD, suggesting that p85 may play a role in helping to anchor pllO within the TFIID complex and, with other studies, that TFHIID assembly and function may involve a concerted series of subunit interactions. Interestingly, the carboxy terminus of p85 contains eight of the WD-40 repeats found originally in the v subunit of G proteins and more recently in other transcriptional regulatory factors. However, truncated p85 lacking all the WD-40 repeats maintained interactions with both TFIDr and p110. Transcription of protein-encoding genes in eukaryotes is regulated by various gene-specific transcriptional factors that bind to distinct DNA elements (for reviews, see references 21 and 23). Although these gene-specific factors are thought to regulate transcription by interacting with the RNA polymerase II transcription machinery, their mechanism of action is poorly understood.Transcription factor TFIID plays a central role in assembly of the basal transcription machinery into a preinitiation complex (for reviews, see references 4 and 23), since TFIID binding to the TATA sequence is the first step and thus provides a foundation for association of the other general initiation factors and RNA polymerase II. Consistent with this key role for TFIID, early studies of the mechanism of action of eukaryotic activators demonstrated physical and functional interactions with native TFIID that in turn facilitated preinitiation complex assembly and function (12,13,30). More recent studies have indicated that TFIID is a large multisubunit complex in both Drosophila (5, 18) and human (1,2,25,26,33) Ltd., Hachioji, Tokyo 192, Japan. other components of the preinitiation complex to facilitate either assembly or function.A further understanding of TFIID structure and function will require cloning and expression of cDNAs encoding the different subunits, as well as studies of various proteinprotein interactions and structure-function relationships. Toward this goal, we earlier purified a native TFIID complex from Drosophila embryo extracts by immunoaffinity chromatography with anti-TFIIDr antibody and identified nine tightly associated polypeptides (230, 110, 85, 62, 58, 42,28,22, and 21 kDa) as candidates for TFIID subunits (18). Some but not all of these were also identified in related studies by Dynlacht et al. (5). Cloning and protein-protein interaction studies have been reported for the two largest subunits of TFIID (10,11,16,17,24,28). These include the demonstration of both intramolecular interactions between different TFIID subunits (10,16,17,24,28) and intermolecular...

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“…Analogous to bacterial gene control, recruitment of the core machinery, especially components of the TFIID complex, preoccupied research in the early 1990s (Ptashne and Gann 1997), but other models including conformational changes in TFIID (Horikoshi et al 1988;Hoffmann et al 1997) or nucleosomal rearrangement (Workman et al 1988) were also investigated.…”

Section: Transcription Factors: Local Controlmentioning

confidence: 99%

Epigenetic control: slow and global, nimble and local: Figure 1.

Cheng¹,

Johnson²,

Hoffmann³

2008

Genes Dev.

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The regulation of gene expression involves multiple levels of control, from those that are inheritable to those that are highly responsive to environmental changes. In this issue of Genes & Development, Dong and colleagues (pp. 1159-1173) demonstrate that the dynamically controlled immune response transcription factor NF-B may, in fact, have a role in regulating heterochromatin and gene expression at large distances from its actual target sequences and genes.How the cell regulates the use of its genetic information has been a primary focus of molecular biological research from its inception more than 50 years ago. Two general mechanisms have framed our understanding of how and when the information contained within the DNA is "read" by the cell: those that impede access to the DNA sequence via nucleosome-mediated packaging or DNA methylation, and those mediated by sequence-specific DNA-binding proteins that recruit transcriptional machinery to promoters to activate gene expression. The genome organization into discrete euchromatic and heterochromatic regions (particularly at centromeres, telomeres, and other discrete loci) suggested early on that this packaging was relatively stable and could thereby be inherited to play a key role in development. On the other hand, sequence-specific binding proteins were thought to mediate more nimble, gene-specific control in response to rapidly changing cellular environments. Over the past decade, post-translational modifications of histone tails have emerged as the central regulation step in both types of control, operating at different spatial/temporal scales: the "global" scale that regulates portions of a chromosome at sub-cell cycle time scales, and the "local" scale regulating single transcription units to satisfy dynamically changing physiological needs. However, in this issue of Genes & Development, Dong et al. (2008) provide evidence that suggests a provocative connection between a dynamically regulated transcription factor capable of activating specific target genes, and nonlocal control of gene repression. Heterochromatin: global controlThe term "epigenetics" was coined by Conrad Waddington (Waddington 1942) to account for mechanisms by which genetic information is selectively used as cells differentiate into more specialized functions. The concept of an epigenetic landscape is predicated on the idea that repressive chromatin compaction leads to deselection of genetic information. This pattern is inherited, leading to progressive restriction of cell fate and resulting in differentiation and development. The characteristic chromatin compaction pattern of Drosophila interphase salivary gland chromosomes-where euchromatic and heterochromatic regions are easily distinguished in the microscope-provided an early visual correlate to the accessible and inaccessible genetic loci. This type of epigenetic regulation encompasses multiple genes, is cell type-specific, and relatively stable-less stable than genetic information itself, but more stable than the cellular regulation ...

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Transcriptional regulation by the immediate early protein of pseudorabies virus during in vitro nucleosome assembly

Cited by 181 publications

References 53 publications

Transcriptional characteristics of in vitro assembled chromatin assayed by microinjection into Xenopus laevis oocytes

Transcriptional characteristics of in vitro assembled chromatin assayed by microinjection into Xenopus laevis oocytes

Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit.

Epigenetic control: slow and global, nimble and local: Figure 1.

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