Substrate Specificity of the Kinase P-TEFb towards the RNA Polymerase II C-Terminal Domain

Eric B. Gibbs, Tatiana N. Laremore, Grace A. Usher, Bede Portz, Erik C. Cook, Scott A. Showalter

Research output: Contribution to journalArticle

Abstract

The positive transcription elongation factor b (P-TEFb) promotes transcription elongation through phosphorylation of the RNA polymerase II C-terminal domain. This process is not well understood, partly due to difficulties in determining the specificity of P-TEFb toward the various heptad repeat motifs within the C-terminal domain. A simple assay using mass spectrometry was developed to identify the substrate specificity of the Drosophila melanogaster P-TEFb (DmP-TEFb) in vitro. This assay demonstrated that DmP-TEFb preferentially phosphorylates Ser5 and, surprisingly, that pre-phosphorylation or conserved amino acid variation at the 7-position in the heptad can alter DmP-TEFb specificity, leading to the creation of distinct double-phosphorylation marks.

Original languageEnglish (US)
Pages (from-to)1909-1911
Number of pages3
JournalBiophysical journal
Volume113
Issue number9
DOIs
StatePublished - Nov 7 2017

All Science Journal Classification (ASJC) codes

  • Biophysics

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