ArticleProceedings of the National Academy of Sciences of the United States of America2005
Transcriptional activating regions target attached substrates to a cyclin-dependent kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Quantitative modelling of P-TEFb mediated CTD phosphorylation identifies local cooperativity.PLoS computational biology · 2026Article
- Multiple roles of CTDK-I throughout the cell.Cellular and molecular life sciences : CMLS · 2019Review
- Noncanonical CTD kinases regulate RNA polymerase II in a gene-class-specific manner.Nature chemical biology · 2019Article
- The mRNA capping enzyme of Saccharomyces cerevisiae has dual specificity to interact with CTD of RNA Polymerase II.Scientific reports · 2016Article
- Pathway connectivity and signaling coordination in the yeast stress-activated signaling network.Molecular systems biology · 2014Article
- Chemical-genomic dissection of the CTD code.Nature structural & molecular biology · 2010Article
- TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II.Molecular cell · 2009Article
- The Mediator complex and transcription regulation.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast cyclin-dependent kinase Srb10 phosphorylates various transcriptional activators as they activate transcription, and acidic transcriptional activating domains found on several activators directly bind Srb10. Here we show that the interaction between Srb10 (with its associated cyclin Srb11) and each of several different activating regions, in vitro, leads to the phosphorylation of peptide sequences attached to but outside of the activating regions themselves. In some cases, residues within the activating regions are also phosphorylated. The results define a mechanism by which a kinase is recruited to alternate substrates with diverse physiological consequences.
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