Mayfield, J.E., et al., (2019).
Tyr1 phosphorylation promotes phosphorylation of Ser2 on the C-terminal domain of eukaryotic RNA polymerase II by P-TEFb. eLife

Naowarojan, N., et al., (2019)
Crystal Structure of the Ergothioneine Sulfoxide Synthase from Candidatus Chloracidobacterium thermophilum and Structure-Guided Engineering To Modulate Its Substrate Selectivity.ACS Catal.

Baas, B., et al., (2019).
Structural, Kinetic, and Mechanistic Analysis of an Asymmetric 4-Oxalocrotonate Tautomerase Trimer. Biochemistry.

Irani, S., et. al., (2019).
Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate CTD phosphatase during eukaryotic transcription. Jour. of Biol. Chem.

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The transcription process in eukaryotic cells is controlled by the C-terminal domain of RNA polymerase II through its post-translational modification states. However enzymes that recognize the same phosphorylation site in CTD can lead to different transcriptional outcomes. To address the central question that how gene-specific regulation was achieved by CTD regulatory enzymes, we investigate the structure function mechanism of CTD phosphatases. Specifically, a protein regulation prolyl isomerization state of the CTD proline residues can affect the transcription by controlling the availability of the substrate pools for the phosphatases. We also develop chemical compounds as tools to understand the proline isomerization state specificity of CTD binding enzymes and chemical probes to promote neuron regeneration.

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