Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases

Stéhane Hausmann, Hisashi Koiwa, Shankarling Krishnamurthy, Michael Hampsey, Stewart Shuman

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

The phosphorylated carboxyl-terminal domain (CTD) of RNA polymerase II, consisting of (1YSPTSPS7)n heptad repeats, encodes information about the state of the transcriptional apparatus that can be conveyed to factors that regulate mRNA synthesis and processing. Here we describe how the CTD code is read by two classes of protein phosphatases, plant CPLs and yeast Ssu72, that specifically dephosphorylate Ser5 in vitro. The CPLs and Ssu72 recognize entirely different positional cues in the CTD primary structure. Whereas the CPLs rely on Tyr1 and Pro 3 located on the upstream side of the Ser5-PO4 target site, Ssu72 recognizes Thr4 and Pro6 flanking the target Ser5-PO4 plus the downstream Tyr1 residue of the adjacent heptad. We surmise that the reading of the CTD code does not obey uniform rules with respect to the location and phasing of specificity determinants. Thus, CTD code, like the CTD structure, is plastic.

Original languageEnglish (US)
Pages (from-to)37681-37688
Number of pages8
JournalJournal of Biological Chemistry
Volume280
Issue number45
DOIs
StatePublished - Nov 11 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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