Structural Motifs for CTD Kinase Specificity on RNA Polymerase II during Eukaryotic Transcription.

ABSTRACT: The phosphorylation states of RNA polymerase II coordinate the process of eukaryotic transcription by recruitment of transcription regulators. The individual residues of the repetitive heptad of the C-terminal domain (CTD) of the biggest subunit of RNA polymerase II are phosphorylated temporally at different stages of transcription. Intriguingly, despite similar flanking residues, phosphorylation of Ser2 and Ser5 in CTD heptads play dramatically different roles. The mechanism of how the kinases place phosphorylation on the correct serine is not well understood. In this paper, we use biochemical assays, mass spectrometry, molecular modeling, and structural analysis to understand the structural elements determining which serine of the CTD heptad is subject to phosphorylation. We identified t

SUBMITTER: Ramani MKV 

PROVIDER: S-EPMC8018230 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature