Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast

Kayne, Paul S.; Kim, Ung-Jin; Han, Min; Mullen, Janet R.; Yoshizaki, Fuminori; Grunstein, Michael

doi:10.1016/0092-8674(88)90006-2

Cited by 419 publications

(304 citation statements)

References 48 publications

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“…2A) and GAL4(1-100 ϩ 840-857) (Ryan and Morse, unpublished) showed significant activation. These results were obtained by using the GAL4-TBP expression vector of Xiao et al (79) in strain CY296; essentially identical results were obtained in the yeast strain PKY999 (35) by using the expression vector for GAL4-TBP we constructed ourselves, which was used in Fig. 1 (Ryan and Morse, unpublished).…”

Section: Retention Of Tbp Function In a Gal4-tbp Fusionsupporting

confidence: 60%

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Ryan

Stafford

et al. 2000

Molecular and Cellular Biology

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Transcriptional activators are believed to work in part by recruiting general transcription factors, such as TATA-binding protein (TBP) and the RNA polymerase II holoenzyme. Activation domains also contribute to remodeling of chromatin in vivo. To determine whether these two activities represent distinct functions of activation domains, we have examined transcriptional activation and chromatin remodeling accompanying artificial recruitment of TBP in yeast (Saccharomyces cerevisiae). We measured transcription of reporter genes with defined chromatin structure by artificial recruitment of TBP and found that a reporter gene whose TATA element was relatively accessible could be activated by artificially recruited TBP, whereas two promoters, GAL10 and CHA1, that have accessible activator binding sites, but nucleosomal TATA elements, could not. A third reporter gene containing the HIS4 promoter could be activated by GAL4-TBP only when a RAP1 binding site was present, although RAP1 alone could not activate the reporter, suggesting that RAP1 was needed to open the chromatin structure to allow activation. Consistent with this interpretation, artificially recruited TBP was unable to perturb nucleosome positioning via a nucleosomal binding site, in contrast to a true activator such as GAL4, or to perturb the TATA-containing nucleosome at the CHA1 promoter. Finally, we show that activation of the GAL10 promoter by GAL4, which requires chromatin remodeling, can occur even in swi gcn5 yeast, implying that remodeling pathways independent of GCN5, the SWI-SNF complex, and TFIID can operate during transcriptional activation in vivo.Transcriptional activators are thought to stimulate transcription of TATA-containing promoters in part by recruiting TFIID, a multiprotein complex consisting of the TATA-binding protein (TBP) and TBP-associated factors (TAFs), to the TATA box (25,60). Several in vitro and in vivo studies support this model. For example, transcription initiated at a mutated TATA element by induced synthesis of TBP with altered specificity was enhanced in both rate and extent in the presence of an activator that could bind upstream of the relevant promoter, consistent with activator-mediated recruitment (40). Recruitment has also been inferred from the results of "activator bypass" experiments in which artificial recruitment of TBP to promoter sites near the TATA element resulted in transcriptional activation, implying that TBP recruitment is a rate-limiting step in transcriptional activation in vivo (10,39,79). Most convincingly, chromatin immunoprecipitation experiments revealed TBP to be physically associated with promoters of numerous genes under activated, but not nonactivated, conditions, implying that recruitment accompanies activation (43,46).A potential obstacle to recruitment of TBP in vivo is posed by chromatin. Binding of TBP to nucleosomal TATA elements is greatly impeded in vitro (23, 32). Transcription is also strongly repressed by chromatin, but this repression can be largely alleviated by binding of act...

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Section: Retention Of Tbp Function In a Gal4-tbp Fusionsupporting

confidence: 60%

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Ryan

Stafford

et al. 2000

Molecular and Cellular Biology

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“…This is strongly supported by the observation that a deletion of the histone H2B cross-linking domain changes the minichromosome topology in vivo, suggesting that this domain is required for the proper folding of DNA in the nucleosome (63). Deletion or substitution of a single amino acid in the cross-linking domain of histone H4 alters chromatin structure in vivo (63)(64)(65)(66), decreases the ability of yeast to mate, increases the duration of S phase (67)(68)(69)(70), and affects telomeric repression (71,72) as well as expression of a large number of yeast genes (64,65,(73)(74)(75). It should be mentioned also that the cross-linking domain of histone H4 contains sites for post-translational acetylation and phosphorylation (76) that may also be involved in the regulation of the interaction of this domain with DNA at different levels of chromatin activity and condensation rendering nucleosomes competent for transcription and/or replication.…”

Section: The Change In Histone H2b/h4-dna Contacts Induced By Low Ionmentioning

confidence: 49%

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Gavin¹,

Usachenko²,

Bavykin

1998

Journal of Biological Chemistry

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We have recently reported that certain core histone-DNA contacts are altered in nucleosomes during chromatin unfolding (Usachenko, S. I., Gavin I. M., and Bavykin, S. G. (1996) J. Biol. Chem. 271, 3831-3836). In this work, we demonstrate that these alterations are caused by a conformational change in the nucleosomal DNA. Using zero-length protein-DNA cross-linking, we have mapped histone-DNA contacts in isolated core particles at ionic conditions affecting DNA stiffness, which may change the nucleosomal DNA conformation. We found that the alterations in histone-DNA contacts induced by an increase in DNA stiffness in isolated core particles are identical to those observed in nucleosomes during chromatin unfolding. The change in the pattern of micrococcal nuclease digestion of linker histone-depleted chromatin at ionic conditions affecting chromatin compaction also suggests that the stretching of the linker DNA may alter the nucleosomal DNA conformation, resulting in a structural transition in the nucleosome which may play a role in rendering the nucleosome competent for transcription and/or replication.

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“…Alternatively, these alterations may arise through phosphorylation of histones. Elegant studies with Saccharomyces cerevisiae have shown that histone tails, which are highly basic and contain sites for acetylation and phosphorylation (reviewed in reference 11), can play a role in transcriptional regulation, most likely through interactions with soluble transcription factors and/or repressors (24,31,33,39,56). Various effectors have been shown to induce changes in histone phosphorylation in mammalian cells (1,19,38,40,62).…”

Section: Discussionmentioning

confidence: 99%

Nucleoprotein Structure Influences the Response of the Mouse Mammary Tumor Virus Promoter to Activation of the Cyclic AMP Signalling Pathway

Pennie

Hager

Smith

1995

Molecular and Cellular Biology

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Recent studies have provided evidence of crosstalk between steroid receptors and cyclic AMP (cAMP) signalling pathways in the regulation of gene expression. A synergism between intracellular phosphorylation inducers and either glucocorticoids or progestins has been shown to occur during activation of the mouse mammary tumor virus (MMTV) promoter. We have investigated the effect of 8-Br-cAMP and okadaic acid, modulators of cellular kinases and phosphatases, on the hormone-induced activation of the MMTV promoter in two forms: a transiently transfected template with a disorganized, accessible nucleoprotein structure and a stably replicating template with an ordered, inaccessible nucleoprotein structure. Both okadaic acid and 8-Br-cAMP synergize significantly with either glucocorticoids or progestins in activating the transiently transfected MMTV template. In contrast, 8-Br-cAMP, but not okadaic acid, is antagonistic to hormoneinduced activation of the stably replicating MMTV template. Nuclear run-on experiments demonstrate that this inhibition is a transcriptional effect on both hormone-induced transcription and basal transcription. Surprisingly, 8-Br-cAMP does not inhibit glucocorticoid-induced changes in restriction enzyme access and nuclear factor 1 binding. However, association of a complex with the TATA box region is inhibited in the presence of 8-Br-cAMP. Thus, cAMP treatment interferes with the initiation process but does not inhibit interaction of the receptor with the template. Since the replicated, ordered MMTV templates and the transfected, disorganized templates show opposite responses to 8-Br-cAMP treatment, we conclude that chromatin structure can influence the response of a promoter to activation of the cAMP signalling pathway.The mouse mammary tumor virus long terminal repeat (MMTV LTR) has been used extensively as a model for both steroid-induced transcription and the effects of chromatin structure on transcription. The MMTV promoter can be activated by glucocorticoids, progestins, androgens, and mineralocorticoids through their individual receptors (8,18,21,55). In chromatin, the MMTV LTR exists as an ordered array of six nucleosomes, one of which (Nuc-B) is associated with the promoter region containing binding sites for glucocorticoid receptor (GR) and nuclear factor 1 (NF1) (54). In the absence of activated GR, the MMTV chromatin template is found to be in a ''closed'' architecture, with the transcription factors NF1 and OTF1 largely occluded from their high-affinity binding sites (20,35). Upon treatment with glucocorticoids, the Nuc-B region undergoes a structural transition which results in an opening of chromatin structure, characterized by increased nuclease accessibility and the binding of NF1, OTF1, and the basal transcriptional machinery (4,20,35,54). These observations suggested a bimodal model of MMTV transcriptional activation (6), in which nucleoprotein structure limits the access of transcription factors to their sites on MMTV chromatin in the absence of hormone. This repression is ...

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Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast

Cited by 419 publications

References 48 publications

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Nucleoprotein Structure Influences the Response of the Mouse Mammary Tumor Virus Promoter to Activation of the Cyclic AMP Signalling Pathway

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