Molecular Topology of RNA Polymerase I Upstream Activation Factor.
| Autor: | Knutson BA; SUNY Upstate Medical University, Department of Biochemistry and Molecular Biology, Syracuse, New York, USA Knutsonb@upstate.edu., Smith ML; SUNY Upstate Medical University, Department of Biochemistry and Molecular Biology, Syracuse, New York, USA., Belkevich AE; SUNY Upstate Medical University, Department of Biochemistry and Molecular Biology, Syracuse, New York, USA., Fakhouri AM; SUNY Upstate Medical University, Department of Biochemistry and Molecular Biology, Syracuse, New York, USA. |
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| Jazyk: | angličtina |
| Zdroj: | Molecular and cellular biology [Mol Cell Biol] 2020 Jun 15; Vol. 40 (13). Date of Electronic Publication: 2020 Jun 15 (Print Publication: 2020). |
| DOI: | 10.1128/MCB.00056-20 |
| Abstrakt: | Upstream activation factor (UAF) is a multifunctional transcription factor in Saccharomyces cerevisiae that plays dual roles in activating RNA polymerase I (Pol I) transcription and repression of Pol II. For Pol I, UAF binds to a specific upstream element in the ribosomal DNA (rDNA) promoter and interacts with two other Pol I initiation factors, the TATA-binding protein (TBP) and core factor (CF). We used an integrated combination of chemical cross-linking mass spectrometry (CXMS), molecular genetics, protein biochemistry, and structural modeling to understand the topological framework responsible for UAF complex formation. Here, we report the molecular topology of the UAF complex, describe new structural and functional domains that play roles in UAF complex integrity, assembly, and biological function, and provide roles for previously identified UAF domains that include the Rrn5 SANT and histone fold domains. We highlight the role of new domains in Uaf30 that include an N-terminal winged helix domain and a disordered tethering domain as well as a BORCS6-like domain found in Rrn9. Together, our results reveal a unique network of topological features that coalesce around a histone tetramer-like core to form the dual-function UAF complex. (Copyright © 2020 American Society for Microbiology.) |
| Databáze: | MEDLINE |
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