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  A structural perspective of CTD function.

Meinhart, A., Kamenski, T., Hoeppner, S., Baumli, S., & Cramer, P. (2005). A structural perspective of CTD function. Genes and Development, 19(12), 1401-1415. doi:10.1101/gad.1318105.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-847E-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C16D-E
Genre: Journal Article

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1940606.pdf (Publisher version), 506KB
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 Creators:
Meinhart, A., Author
Kamenski, T., Author
Hoeppner, S., Author
Baumli, S., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: The C-terminal domain (CTD) of RNA polymerase II (Pol II) integrates nuclear events by binding proteins involved in mRNA biogenesis. CTD-binding proteins recognize a specific CTD phosphorylation pattern, which changes during the transcription cycle, due to the action of CTD-modifying enzymes. Structural and functional studies of CTD-binding and -modifying proteins now reveal some of the mechanisms underlying CTD function. Proteins recognize CTD phosphorylation patterns either directly, by contacting phosphorylated residues, or indirectly, without contact to the phosphate. The catalytic mechanisms of CTD kinases and phosphatases are known, but the basis for CTD specificity of these enzymes remains to be understood.

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Language(s): eng - English
 Dates: 2005-06
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1101/gad.1318105
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Title: Genes and Development
Source Genre: Journal
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Pages: - Volume / Issue: 19 (12) Sequence Number: - Start / End Page: 1401 - 1415 Identifier: -