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- W3175796924 abstract "The goal of this project is to study the structure and function of the C-terminal domain of RNA Polymerase II (CTD). The CTD, which contains tandem repeats of the consensus heptad sequence YSPTSPS, orchestrates transcription by recruiting trans-acting regulatory factors, directed by a set of post-translational modifications known as the CTD code. Since the discovery of the CTD code, much effort has gone into the identification of novel modifications, the determination of their effects on specific CTD interactions, and the structural characterization of transcription factors in complex with the CTD. Much less is known about the CTD in its unbound state and of the possible structural effects of the post-translational modifications that constitute the code. Recently, we have begun biophysical characterization of the unmodified and hyperphosphorylated CTD using a combination of techniques, including 13C Direct-Detect Nuclear Magnetic Resonance (NMR) spectroscopy and Mass Spectrometry. Preliminary results suggest that the CTD exists in an extended conformation that cannot be adequately described by the previously proposed beta–spiral model. The models we have developed serve as novel structural hypothesis, relevant for determination of the structural basis for the CTD code and the elucidation of the molecular mechanisms of eukaryotic transcription. This work is funded by NSF CAREER award (MCB-0953918) to Scott A. Showalter." @default.
- W3175796924 created "2021-07-05" @default.
- W3175796924 creator A5047930774 @default.
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- W3175796924 date "2015-04-01" @default.
- W3175796924 modified "2023-09-27" @default.
- W3175796924 title "Investigating the Structural Basis of the CTD Code" @default.
- W3175796924 doi "https://doi.org/10.1096/fasebj.29.1_supplement.712.13" @default.
- W3175796924 hasPublicationYear "2015" @default.
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