Structural insights to how mammalian capping enzyme reads the CTD code Journal Article


Authors: Ghosh, A.; Shuman, S.; Lima, C.
Article Title: Structural insights to how mammalian capping enzyme reads the CTD code
Abstract: Physical interaction between the phosphorylated RNA polymerase II carboxyl-terminal domain (CTD) and cellular capping enzymes is required for efficient formation of the 5′ mRNA cap, the first modification of nascent mRNA. Here, we report the crystal structure of the RNA guanylyltransferase component of mammalian capping enzyme (Mce) bound to a CTD phosphopeptide. The CTD adopts an extended β-like conformation that docks Tyr1 and Ser5-PO4 onto the Mce nucleotidyltransferase domain. Structure-guided mutational analysis verified that the Mce-CTD interface is a tunable determinant of CTD binding and stimulation of guanylyltransferase activity, and of Mce function in vivo. The location and composition of the CTD binding site on mammalian capping enzyme is distinct from that of a yeast capping enzyme that recognizes the same CTD primary structure. Thus, capping enzymes from different taxa have evolved different strategies to read the CTD code. © 2011 Elsevier Inc.
Journal Title: Molecular Cell
Volume: 43
Issue: 2
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2011-07-22
Start Page: 299
End Page: 310
Language: English
DOI: 10.1016/j.molcel.2011.06.001
PROVIDER: scopus
PMCID: PMC3142331
PUBMED: 21683636
DOI/URL:
Notes: --- - "Export Date: 17 August 2011" - "CODEN: MOCEF" - "Source: Scopus"
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  1. Stewart H Shuman
    546 Shuman
  2. Agnidipta Ghosh
    6 Ghosh
  3. Christopher D Lima
    103 Lima