FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2588387166> ?p ?o ?g. }

• W2588387166 abstract "Timothy Hoey, Robert 0. J. Weinzierl, Grace Gill, Jin-Long Chen, Brian David Dynlacht, and Robert Tjian Howard Hughes Medical Institute Department of Molecular and Cell Biology University of California at Berkeley Berkeley, California 94720 Summary The general transcription factor TFIID is a multiprotein complex containing the TATA-binding protein and sev- eral associated factors (TAFs), some of which may function as coactivators that are essential for acti- vated, but not basal, transcription. Here we describe the isolation and characterization of the first gene en- coding a TAF protein. The deduced amino acid se- quence of TAFllO revealed the presence of several glutamine- and serinelthreonine-rich regions reminis- cent of the protein-protein interaction domains of the regulatory transcription factor Spl that are involved in transcription activation and multimerization. In both Drosophila cells and yeast, TAFl 10 specifically inter- acts with the glutamincrich activation domains of Spl . Moreover, purified Spl selectively binds recombinant TAFllO in vitro. These findings taken together sug- gest that TAFllO may function as a coactivator by serving as a site of protein-protein contact between activators like Spl and the TFIID complex. Introduction How do sequence-specific DNA binding factors communi- cate with the transcriptional machinery to regulate rates of transcriptional initiation? A model that has gained increas- ing acceptance proposes that site-specific transcriptional activators and repressors interact directly with one or more of the accessory proteins that form the initiation complex assembled at the promoter (for reviews see Gill and Tjian, 1992; Roeder, 1991). It is, at present, unknown whether ail RNA polymerase II regulatory factors work via a common mechanism during the assembly of an active initiation complex or whether different transcriptional activators function by interacting with different target proteins in the initiation complex. To study the mechanisms involved in transcriptional control, the specific components required to assemble an activated transcriptional complex must first be biochemically defined. In recent years, aconcerted effort has been devoted to the purification, characteriza- tion, and subsequent molecular cloning of the genes en- coding all of the components of the transcription machin- ery for RNA poiymerase Ii (TFIIA, B, D, E, F, and H; for review see Zawei and Reinberg, 1992). These studies have, in some instances, revealed unexpected results that have profoundly altered our view of how activation of tran- scription occurs. For example, the cloning of the TATA- binding protein (TBP) gene led to the finding that TFIID is not a single protein, as had been generally assumed. Instead, in higher eukaryotes, TFIID consists of a multisub- unit complex containing the TBP and at least seven distinct and tightly associated factors, called TAFs (Dynlacht et al., 1991; Tanese et 1991). An important property of TAFs is that they are essential for mediating regulated transcription but are not required for basal activity. Thus, TAFs have the biochemical activi- ties expected of coactivators (Dynlacht et al., 1991; Tanese et al., 1991). It is not known how TAFs or coactiva- tors function to mediate regulated transcription, nor is it known whether ail TAFs serve as coactivators. In the sim- plest model, we originally proposed that coactivator pro- teins could serve as adaptor molecules connecting the activation domains of regulatory factors and the basal tran- scriptional machinery (Pugh and Tjian, 1990), and we speculated that perhaps different classes of activators have different coactivator requirements. Studies in yeast have identified an activity, termed a mediator or adaptor, that may function as a bridging protein between the tran- scriptional activator VP16 and the basal factors there- fore may be similar to coactivators (Berger et al., 1990; Kelleher et al., 1990; Flanagan et al., 1991). Unlike TAFs, the adaptor or mediator proteins in yeast do not appear to be stably associated with TBP, which can be purified from yeast as a free protein (Buratowski et al., 1988). Eukaryotic transcription factors have a modular design with separable DNA-binding and activation domains (for review see Frankel and Kim, 1991). Transcriptional activa- tion domains can be thought of as those parts of regulatory factors that are specialized for protein-protein interaction with some component of the transcription initiation com- plex. Transcriptional activation domains are typically di- vided into three major classes based on their amino acid sequences: those rich in acidic, glutamine, or proline resi- dues (for review see Mitchell and Tjian, 1989). It is, at present, unknown whether these classifications reflect any significant structural or functional features of activa- tion domains. The VP16 activation domain, considered to be the prototype for the acidic class of activators, has been reported to interact with TBP (Stringer et al., 1990) and TFIIB (Lin et al., 1991) by in vitro binding assays, although the importance of these interactions in assembly an activated transcription complex remains unclear. Thus far, no potential targets for proline or glutamine-rich activation domains have been identified by direct binding studies. Human transcription factor Spl contains two glutamine- rich activation domains that can function as potent activa- tors (Courey and Tjian, 1988). We have used Spl as a prototype activator for investigating the mechanisms of regulation by eukaryotic transcription factors. In addition, recent studies reveal that these glutamine-rich activation domains of Spl also function as protein-protein interac- tion surfaces for the formation of homomultimers (Pascal and Tjian, 1991) as well as interfaces for interactions with the basal machinery. In this report, we describe a specific component of the" @default.
• W2588387166 created "2017-02-24" @default.
• W2588387166 creator A5020711185 @default.
• W2588387166 creator A5041905160 @default.
• W2588387166 creator A5054610344 @default.
• W2588387166 creator A5079033247 @default.
• W2588387166 creator A5082330841 @default.
• W2588387166 creator A5087723552 @default.
• W2588387166 date "1993-01-01" @default.
• W2588387166 modified "2023-09-24" @default.
• W2588387166 title "lkdecular Cloning and Functionai Anatysis of0 ila TAFI 10 Rev& Expec4ed of Coactiiators" @default.
• W2588387166 cites W1967208634 @default.
• W2588387166 cites W1971227936 @default.
• W2588387166 cites W1974850260 @default.
• W2588387166 cites W1977186059 @default.
• W2588387166 cites W1979344499 @default.
• W2588387166 cites W1983642216 @default.
• W2588387166 cites W1985001103 @default.
• W2588387166 cites W1986251535 @default.
• W2588387166 cites W1986390248 @default.
• W2588387166 cites W1993125057 @default.
• W2588387166 cites W1996251138 @default.
• W2588387166 cites W1999738251 @default.
• W2588387166 cites W2002554363 @default.
• W2588387166 cites W2004636267 @default.
• W2588387166 cites W2005573768 @default.
• W2588387166 cites W2007675804 @default.
• W2588387166 cites W2013980278 @default.
• W2588387166 cites W2015617558 @default.
• W2588387166 cites W2016736163 @default.
• W2588387166 cites W2021893003 @default.
• W2588387166 cites W2027216583 @default.
• W2588387166 cites W2037653294 @default.
• W2588387166 cites W2040193953 @default.
• W2588387166 cites W2045545244 @default.
• W2588387166 cites W2053700118 @default.
• W2588387166 cites W2059963899 @default.
• W2588387166 cites W2062439115 @default.
• W2588387166 cites W2063767041 @default.
• W2588387166 cites W2065679706 @default.
• W2588387166 cites W2068577315 @default.
• W2588387166 cites W2074351361 @default.
• W2588387166 cites W2075263567 @default.
• W2588387166 cites W2079557259 @default.
• W2588387166 cites W2081085542 @default.
• W2588387166 cites W2085206941 @default.
• W2588387166 cites W2086470847 @default.
• W2588387166 cites W2089126365 @default.
• W2588387166 cites W2090509456 @default.
• W2588387166 cites W2092609742 @default.
• W2588387166 cites W2126020531 @default.
• W2588387166 cites W2130258789 @default.
• W2588387166 cites W2136690570 @default.
• W2588387166 cites W2140134113 @default.
• W2588387166 cites W2152927202 @default.
• W2588387166 cites W2156071334 @default.
• W2588387166 cites W2161585446 @default.
• W2588387166 hasPublicationYear "1993" @default.
• W2588387166 type Work @default.
• W2588387166 sameAs 2588387166 @default.
• W2588387166 citedByCount "0" @default.
• W2588387166 crossrefType "journal-article" @default.
• W2588387166 hasAuthorship W2588387166A5020711185 @default.
• W2588387166 hasAuthorship W2588387166A5041905160 @default.
• W2588387166 hasAuthorship W2588387166A5054610344 @default.
• W2588387166 hasAuthorship W2588387166A5079033247 @default.
• W2588387166 hasAuthorship W2588387166A5082330841 @default.
• W2588387166 hasAuthorship W2588387166A5087723552 @default.
• W2588387166 hasConcept C101762097 @default.
• W2588387166 hasConcept C102622118 @default.
• W2588387166 hasConcept C104317684 @default.
• W2588387166 hasConcept C111936080 @default.
• W2588387166 hasConcept C138885662 @default.
• W2588387166 hasConcept C144825837 @default.
• W2588387166 hasConcept C146027311 @default.
• W2588387166 hasConcept C150194340 @default.
• W2588387166 hasConcept C153911025 @default.
• W2588387166 hasConcept C158448853 @default.
• W2588387166 hasConcept C172768829 @default.
• W2588387166 hasConcept C179926584 @default.
• W2588387166 hasConcept C41895202 @default.
• W2588387166 hasConcept C44498088 @default.
• W2588387166 hasConcept C54355233 @default.
• W2588387166 hasConcept C65888428 @default.
• W2588387166 hasConcept C77445288 @default.
• W2588387166 hasConcept C86339819 @default.
• W2588387166 hasConcept C86803240 @default.
• W2588387166 hasConcept C95444343 @default.
• W2588387166 hasConceptScore W2588387166C101762097 @default.
• W2588387166 hasConceptScore W2588387166C102622118 @default.
• W2588387166 hasConceptScore W2588387166C104317684 @default.
• W2588387166 hasConceptScore W2588387166C111936080 @default.
• W2588387166 hasConceptScore W2588387166C138885662 @default.
• W2588387166 hasConceptScore W2588387166C144825837 @default.
• W2588387166 hasConceptScore W2588387166C146027311 @default.
• W2588387166 hasConceptScore W2588387166C150194340 @default.
• W2588387166 hasConceptScore W2588387166C153911025 @default.
• W2588387166 hasConceptScore W2588387166C158448853 @default.
• W2588387166 hasConceptScore W2588387166C172768829 @default.
• W2588387166 hasConceptScore W2588387166C179926584 @default.

• next