Various in vivo and in vitro assays have been employed to analyze how activators communicate with the general transcription machinery to stimulate transcription. As a first step, I analyzed the function of distinct kinds of activation domains in yeast and human. The results showed that the proline-rich activation domain of CTF1 can, like acidic activation domains, activate transcription in yeast and human. Based on this, I compared the activation pathways by acidic and proline-rich activation domains in yeast and human. These detailed comparative approaches yielded clues to the fundamental aspects of transcriptional activation mechanism in eukaryotes: activators target TFIID (TBP)-TFIIB promoter complex formation in the preinitiation complex assembly process by inducing (or stabilizing) qualitative or quantitative alterations within TFIID (TBP)-TFIIB-promoter complexes that consequently enhance recruitment of downstream initiation factors. Consistent with this view, various activation domains have been demonstrated to have physical and functional interactions with TBP and/or TFIIB. Given the central role of TBP in transcriptional regulation, I also identified distinct TBP domains (or residues) important for different regulatory interactions including those with acidic activators, TFIIB, Dr1 (NC2), Pol I- and Pol III- specific factors. These mutational analyses have provided an insight into how the interplay of many regulatory factors occurs on the surface of a target factor, TBP, to specify and regulate transcriptional activity. Furthermore, I investigated the essential features of the CTF1 proline-rich activation domain and showed that CTD-like sequences (Ser-Pro motifs) are important for activation, possibly by forming a β-turned omega (Ω) loop structure. Thus, the β-turn structure is likely to be a salient secondary structure in the activation domains in addition to a β-sheet structure which was previously proposed for acidic activation domains.
","abstract_html":"<p>Various in vivo and in vitro assays have been employed to analyze how activators communicate with the general transcription machinery to stimulate transcription. As a first step, I analyzed the function of distinct kinds of activation domains in yeast and human. The results showed that the proline-rich activation domain of CTF1 can, like acidic activation domains, activate transcription in yeast and human. Based on this, I compared the activation pathways by acidic and proline-rich activation domains in yeast and human. These detailed comparative approaches yielded clues to the fundamental aspects of transcriptional activation mechanism in eukaryotes: activators target TFIID (TBP)-TFIIB promoter complex formation in the preinitiation complex assembly process by inducing (or stabilizing) qualitative or quantitative alterations within TFIID (TBP)-TFIIB-promoter complexes that consequently enhance recruitment of downstream initiation factors. Consistent with this view, various activation domains have been demonstrated to have physical and functional interactions with TBP and/or TFIIB. Given the central role of TBP in transcriptional regulation, I also identified distinct TBP domains (or residues) important for different regulatory interactions including those with acidic activators, TFIIB, Dr1 (NC2), Pol I- and Pol III- specific factors. These mutational analyses have provided an insight into how the interplay of many regulatory factors occurs on the surface of a target factor, TBP, to specify and regulate transcriptional activity. Furthermore, I investigated the essential features of the CTF1 proline-rich activation domain and showed that CTD-like sequences (Ser-Pro motifs) are important for activation, possibly by forming a β-turned omega (Ω) loop structure. Thus, the β-turn structure is likely to be a salient secondary structure in the activation domains in addition to a β-sheet structure which was previously proposed for acidic activation domains.</p>","abstract_has_math":false,"creators":["Kim, Tae Kook"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":["Robert G. Roeder"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1994,"date_issued":"1994-01-01T08:00:00Z","date_published":"1994-01-01T08:00:00Z","updated_at":"2026-07-24T04:11:55Z","subjects":["transcriptional activation","activation domains","TATA-box binding protein (TBP)","TFIIB","proline-rich domain","beta-turn structure","Life Sciences"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.rockefeller.edu/student_theses_and_dissertations/373","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Robert G. 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As a first step, I analyzed the function of distinct kinds of activation domains in yeast and human. The results showed that the proline-rich activation domain of CTF1 can, like acidic activation domains, activate transcription in yeast and human. Based on this, I compared the activation pathways by acidic and proline-rich activation domains in yeast and human. These detailed comparative approaches yielded clues to the fundamental aspects of transcriptional activation mechanism in eukaryotes: activators target TFIID (TBP)-TFIIB promoter complex formation in the preinitiation complex assembly process by inducing (or stabilizing) qualitative or quantitative alterations within TFIID (TBP)-TFIIB-promoter complexes that consequently enhance recruitment of downstream initiation factors. Consistent with this view, various activation domains have been demonstrated to have physical and functional interactions with TBP and/or TFIIB. Given the central role of TBP in transcriptional regulation, I also identified distinct TBP domains (or residues) important for different regulatory interactions including those with acidic activators, TFIIB, Dr1 (NC2), Pol I- and Pol III- specific factors. These mutational analyses have provided an insight into how the interplay of many regulatory factors occurs on the surface of a target factor, TBP, to specify and regulate transcriptional activity. Furthermore, I investigated the essential features of the CTF1 proline-rich activation domain and showed that CTD-like sequences (Ser-Pro motifs) are important for activation, possibly by forming a β-turned omega (Ω) loop structure. Thus, the β-turn structure is likely to be a salient secondary structure in the activation domains in addition to a β-sheet structure which was previously proposed for acidic activation domains.
"]},{"key":"dc:title","label":"Title","values":["Eukaryotic Transcriptional Activation Mechanism: Protein-Protein Interactions"]}]}],"canonical_facts":{"dc:contributor":["Robert G. Roeder"],"dc:creator":["Kim, Tae Kook"],"dc:description.abstract":["Various in vivo and in vitro assays have been employed to analyze how activators communicate with the general transcription machinery to stimulate transcription. As a first step, I analyzed the function of distinct kinds of activation domains in yeast and human. The results showed that the proline-rich activation domain of CTF1 can, like acidic activation domains, activate transcription in yeast and human. Based on this, I compared the activation pathways by acidic and proline-rich activation domains in yeast and human. These detailed comparative approaches yielded clues to the fundamental aspects of transcriptional activation mechanism in eukaryotes: activators target TFIID (TBP)-TFIIB promoter complex formation in the preinitiation complex assembly process by inducing (or stabilizing) qualitative or quantitative alterations within TFIID (TBP)-TFIIB-promoter complexes that consequently enhance recruitment of downstream initiation factors. Consistent with this view, various activation domains have been demonstrated to have physical and functional interactions with TBP and/or TFIIB. Given the central role of TBP in transcriptional regulation, I also identified distinct TBP domains (or residues) important for different regulatory interactions including those with acidic activators, TFIIB, Dr1 (NC2), Pol I- and Pol III- specific factors. These mutational analyses have provided an insight into how the interplay of many regulatory factors occurs on the surface of a target factor, TBP, to specify and regulate transcriptional activity. Furthermore, I investigated the essential features of the CTF1 proline-rich activation domain and showed that CTD-like sequences (Ser-Pro motifs) are important for activation, possibly by forming a β-turned omega (Ω) loop structure. Thus, the β-turn structure is likely to be a salient secondary structure in the activation domains in addition to a β-sheet structure which was previously proposed for acidic activation domains.
"],"dc:identifier":["https://digitalcommons.rockefeller.edu/student_theses_and_dissertations/373"],"dc:subject":["transcriptional activation","activation domains","TATA-box binding protein (TBP)","TFIIB","proline-rich domain","beta-turn structure","Life Sciences"],"dc:title":["Eukaryotic Transcriptional Activation Mechanism: Protein-Protein Interactions"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T04:11:55Z"}