Document Detail


Structural insights to how mammalian capping enzyme reads the CTD code.
MedLine Citation:
PMID:  21683636     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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-PO(4) 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.
Authors:
Agnidipta Ghosh; Stewart Shuman; Christopher D Lima
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-06-16
Journal Detail:
Title:  Molecular cell     Volume:  43     ISSN:  1097-4164     ISO Abbreviation:  Mol. Cell     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-07-22     Completed Date:  2012-01-03     Revised Date:  2013-12-12    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  299-310     Citation Subset:  IM    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Data Bank Information
Bank Name/Acc. No.:
PDB/3RTX
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Humans
Mammals / genetics,  metabolism
Models, Molecular
Molecular Sequence Data
Mutation
Nucleotidyltransferases / chemistry,  metabolism
Phosphorylation
Protein Structure, Tertiary
RNA Caps / metabolism
RNA Polymerase II / chemistry*,  genetics,  metabolism
Grant Support
ID/Acronym/Agency:
GM052470/GM/NIGMS NIH HHS; GM061906/GM/NIGMS NIH HHS; R01 GM052470/GM/NIGMS NIH HHS; R01 GM061906/GM/NIGMS NIH HHS; R01 GM061906-11A1/GM/NIGMS NIH HHS; R01 GM061906-12/GM/NIGMS NIH HHS; R01 GM061906-13/GM/NIGMS NIH HHS; RR-15301/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/RNA Caps; EC 2.7.7.-/Nucleotidyltransferases; EC 2.7.7.-/RNA Polymerase II; EC 2.7.7.50/mRNA guanylyltransferase
Comments/Corrections
Comment In:
Mol Cell. 2011 Jul 22;43(2):163-5   [PMID:  21777807 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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