The Proteasome Regulatory Particle Alters the SAGA Coactivator to Enhance Its Interactions with Transcriptional Activators

Lee, Daeyoup; Ezhkova, Elena; Li, Bing; Pattenden, Samantha G.; Tansey, William P.; Workman, Jerry L.

doi:10.1016/j.cell.2005.08.015

Cited by 167 publications

(177 citation statements)

References 54 publications

(75 reference statements)

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“…We also demonstrate here that 19 S ATPase activity stimulates Gal4p-SAGA interaction. Consistent with our in vivo data, previous biochemical studies (13) have demonstrated the physical and genetic interactions between SAGA and the 19 S base. Interestingly, we find that Gal4p-SAGA interaction is essential for recruitment of the 19 S base at the GAL1 UAS.…”

Section: Discussionsupporting

confidence: 93%

“…However, the mechanisms by which the proteasome regulates eukaryotic transcriptional activation in a proteolysis-independent manner remain largely unknown. Recent biochemical studies (13,23) have demonstrated the nonproteolytic role of the proteasome in regulation of the activator-coactivator or activator-promoter interaction (and hence transcriptional activation). However, how the 19 S RP regulates transcriptional activation at the promoter is not yet clearly understood in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…1 demonstrate that Gal4p-SAGA interaction is required for recruitment of the 19 S base to the GAL1 UAS. However, a recent biochemical study (13) has demonstrated that the 19 S RP enhances Gal4p-SAGA interaction. How does the 19 S base enhance the Gal4p-SAGA interaction, whereas its recruitment is dependent on Gal4p and SAGA?…”

Section: The 19 S Base But Not Lid or 20 S Cp Is Predominantly Recrmentioning

confidence: 97%

“…Although the mechanisms for the proteolytic role of the proteasome in transcription are relatively well established (28), how the 19 S RP regulates eukaryotic transcriptional activation independently of the 20 S CP is not clearly understood. Recent biochemical studies in yeast (13,23) have implicated the non-proteolytic role of the 19 S RP in regulation of the activator-coactivator/ promoter interactions (and hence transcriptional activation). However, the mechanism of action of the 19 S RP in regulation of eukaryotic transcriptional activation remains unknown in vivo.…”

mentioning

confidence: 99%

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The 19 S Proteasome Subcomplex Establishes a Specific Protein Interaction Network at the Promoter for Stimulated Transcriptional Initiation in Vivo

Malik

Shukla²,

Bhaumik

2009

Journal of Biological Chemistry

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The 26 S proteasome complex that comprises the 20 S core and 19 S regulatory (with six ATPases) particles is engaged in an ATP-dependent degradation of a variety of key regulatory proteins and, thus, controls important cellular processes. Interestingly, several recent studies have implicated the 19 S regulatory particle in controlling eukaryotic transcriptional initiation or activation independently of the 20 S core particle. However, the mechanism of action of the 19 S proteasome subcomplex in regulation of eukaryotic transcriptional activation is not clearly understood in vivo. Here, using a chromatin immunoprecipitation assay in conjunction with mutational and transcriptional analyses in Saccharomyces cerevisiae, we show that the 19 S proteasomal subcomplex establishes a specific protein interaction network at the upstream activating sequence of the promoter. Such an interaction network is essential for formation of the preinitiation complex at the core promoter to initiate transcription. Furthermore, we demonstrate that the formation of the transcription complex assembly at the promoter is dependent on 19 S ATPase activity. Intriguingly, 19 S ATPases appear to cross-talk for stimulation of the assembly of transcription factors at the promoter. Together, these results provide significant insights as to how the 19 S proteasome subcomplex regulates the formation of the active transcription complex assembly (and, hence, transcriptional initiation) at the promoter in vivo.In eukaryotes, transcription is mechanistically divided into different steps such as preinitiation complex (PIC) 4 formation and initiation, elongation, and termination. Transcriptional initiation is an important regulatory step of gene expression, which is greatly stimulated by the gene-specific activators whose recognition sites are present at the upstream region of the promoter. A variety of studies (1-5) indicates that activator interacts directly with one or more components of the transcription machinery to stimulate the assembly of general transcription factors such as TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH as well as RNA polymerase II holoenzyme for formation of the PIC at the core promoter to initiate transcription. Thus, a large number of proteins must interact with each other and with the promoter DNA either directly or indirectly during transcriptional initiation.A growing number of recent studies (6 -28) have implicated the 26 S proteasome complex in controlling and orchestrating the interactions of the transcriptional initiation factors and their localization and abundance in regulating transcriptional initiation or activation. The 26 S proteasome is a highly versatile protein degradation machine with molecular chaperonin activity and consists of a 20 S proteolytic core particle (CP) and a 19 S regulatory particle (RP). The 20 S CP has a cylinder-like structure composed of a stack of two ␣ and two ␤ rings, whereas the 19 S RP comprises a "lid" of eight non-ATPases and a "base" of six ATPases (Rpt1-Rpt6) and three non-ATPases (...

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: The 19 S Base But Not Lid or 20 S Cp Is Predominantly Recrmentioning

confidence: 97%

mentioning

confidence: 99%

See 2 more Smart Citations

The 19 S Proteasome Subcomplex Establishes a Specific Protein Interaction Network at the Promoter for Stimulated Transcriptional Initiation in Vivo

Malik

Shukla²,

Bhaumik

2009

Journal of Biological Chemistry

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“…Others later demonstrated that Rpt6, presumably acting in concert with the other proteins in the 19 S base, is also important in mediating histone modifications and in recruiting the SAGA complex to promoters. Neither of these activities require proteolysis (11,12).…”

mentioning

confidence: 99%

Physical and Functional Interactions of Monoubiquitylated Transactivators with the Proteasome

Archer

Burdine

Liu

et al. 2008

Journal of Biological Chemistry

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Destabilization of activator-DNA complexes by the proteasomal ATPases can inhibit transcription by limiting activator interaction with DNA. Modification of the activator by monoubiquitylation protects the activator from this destabilization activity. In this study, we probe the mechanism of this protective effect of monoubiquitylation. Using novel label transfer and chemical cross-linking techniques, we show that ubiquitin contacts the ATPase complex directly, apparently via Rpn1 and Rpt1. This interaction results in the dissociation of the activation domain-ATPase complex via an allosteric process. A model is proposed in which activator monoubiquitylation serves to limit the lifetime of the activator-ATPase complex interaction and thus the ability of the ATPases to unfold the activator and dissociate the protein-DNA complex.

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Steroid Hormones

Simons¹

2008

Wiley Encyclopedia of Chemical Biology

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Five categories of steroid hormones exist in humans, including androgens, estrogens, glucocorticoids, mineralocorticoids, and progestins. These hormones affect virtually every tissue and organ in the human body and play major roles in the development, differentiation, and homeostasis of normal individuals. Antisteroids usually possess nonsteroidal structures but still block the actions of the steroid hormones and are important tools in endocrine therapies of pathologic conditions. Therefore, how the body regulates where, when, and how much a response to steroids occurs is of major importance. Here we survey what is known about the genomic responses to steroid hormones, each of which is mediated by a unique intracellular receptor protein that interacts with the cellular DNA to modify the rates of gene transcription. These receptors are members of a much larger superfamily of steroid/nuclear receptors, most of which bind either nonsteroidal ligands or no known ligand. Nongenomic (i.e., pathways without initial involvement of genomic DNA) and secondary responses (i.e., changes that require protein synthesis to alter gene transcription) are additional important effects of steroid hormones but are not discussed here. The emphasis is on the biochemistry of the five classes of steroid hormones, the techniques used to study steroid hormone action, and the basic mechanistic steps by which steroids alter gene expression.

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The Proteasome Regulatory Particle Alters the SAGA Coactivator to Enhance Its Interactions with Transcriptional Activators

Cited by 167 publications

References 54 publications

The 19 S Proteasome Subcomplex Establishes a Specific Protein Interaction Network at the Promoter for Stimulated Transcriptional Initiation in Vivo

The 19 S Proteasome Subcomplex Establishes a Specific Protein Interaction Network at the Promoter for Stimulated Transcriptional Initiation in Vivo

Physical and Functional Interactions of Monoubiquitylated Transactivators with the Proteasome

Steroid Hormones

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