The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Phosphorylation and functions of the RNA polymerase II CTD
Open accessAbstract
The C-terminal repeat domain (CTD), an unusual extension appended to the C terminus of the largest subunit of RNA polymerase II, serves as a flexible binding scaffold for numerous nuclear factors; which factors bind is determined by the phosphorylation patterns on the CTD repeats. Changes in phosphorylation patterns, as polymerase transcribes a gene, are thought to orchestrate the association of different sets of factors with the transcriptase and strongly influence functional organization of the nucleus. In this review we appraise what is known, and what is not known, about patterns of phosphorylation on the CTD of RNA polymerases II at the beginning, the middle, and the end of genes; the proposal that doubly phosphorylated repeats are present on elongating polymerase is explored. We discuss briefly proteins known to associate with the phosphorylated CTD at the beginning and ends of genes; we explore in more detail proteins that are recruited to the body of genes, the diversity of their functions, and the potential consequences of tethering these functions to elongating RNA polymerase II. We also discuss accumulating structural information on phosphoCTD-binding proteins and how it illustrates the variety of binding domains and interaction modes, emphasizing the structural flexibility of the CTD. We end with a number of open questions that highlight the extent of what remains to be learned about the phosphorylation and functions of the CTD.
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Citations
Cites
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
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“After initiation, an elongation-phase kinase (CTDK-I in yeast; P-TEFb in metazoa) (Marshall et al. 1996; Lee and Greenleaf 1997) modifies mainly Ser2 residues to generate elongation-proficient RNAPII; elongation-related factors such as Set2 bind to the CTD in this third state of phosphorylation.”
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Batsché, E., Yaniv, M., & Muchardt, C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1030 · Cited by 471
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Is there a code embedded in proteins that is based on post-translational modifications?
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DOT1L and H3K79 Methylation in Transcription and Genomic Stability
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“For example, the hyperphosphorylation of the CTD, principally on Ser5 and Ser2 of the repeats, corresponds to the promoter release of RNAPII and entry into productive transcription elongation, respectively [52].”
BackgroundThe structure and substrate specificity of human Cdk12/Cyclin K
Bösken, C. A., Farnung, L., Hintermair, C., Merzel Schachter, M., Vogel-Bachmayr, K., Blazek, D., Anand, K., Fisher, R. P., Eick, D., & Geyer, M. (2014) · Nature Communications · doi:10.1038/ncomms4505 · Cited by 191
Epigenetic Mechanisms Governing Innate Inflammatory Responses
Perkins, D. J., Patel, M. C., Blanco, J. C. G., & Vogel, S. N. (2016) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2016.0003 · Cited by 51
Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins
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A SWI/SNF-specific Ig-like domain, SWIFT, is a transcription factor binding platform
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Metadata
- Authors
- Phatnani, H. P., & Greenleaf, A. L.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-11-01
- Volume
- 20
- Issue
- 21
- Pages
- 2922-2936
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2045959839
- Cited by
- 752
- References
- 3
- Type
- posted content
- Language
- en
- Open access
- diamond
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