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- W2761347500 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." @default.
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- W2761347500 date "2017-11-01" @default.
- W2761347500 modified "2023-09-29" @default.
- W2761347500 title "Substrate Specificity of the Kinase P-TEFb towards the RNA Polymerase II C-Terminal Domain" @default.
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- W2761347500 doi "https://doi.org/10.1016/j.bpj.2017.09.011" @default.
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