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PMID: 10944120 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex.

The EMBO journal ·Vol. 19 ·No. 16 ·2000-08-15 ·Pages 4372-82

Vilela C, Velasco C, Ptushkina M, McCarthy JE

Abstract

Dcp1 plays a key role in the mRNA decay process in Saccharomyces cerevisiae, cleaving off the 5' cap to leave an end susceptible to exonucleolytic degradation. The eukaryotic initiation factor complex eIF4F, which in yeast contains the core components eIF4E and eIF4G, uses the cap as a binding site, serving as an initial point of assembly for the translation apparatus, and also binds the poly(A) binding protein Pab1. We show that Dcp1 binds to eIF4G and Pab1 as free proteins, as well as to the complex eIF4E-eIF4G-Pab1. Dcp1 interacts with the N-terminal region of eIF4G but does not compete significantly with eIF4E or Pab1 for binding to eIF4G. Most importantly, eIF4G acts as a function-enhancing recruitment factor for Dcp1. However, eIF4E blocks this effect as a component of the high affinity cap-binding complex eIF4E-eIF4G. Indeed, cooperative enhancement of the eIF4E-cap interaction stabilizes yeast mRNAs in vivo. These data on interactions at the interface between translation and mRNA decay suggest how events at the 5' cap and 3' poly(A) tail might be coupled.

MeSH Terms
Blotting, Western Chromatography, Agarose Cross-Linking Reagents/pharmacology Electrophoresis, Polyacrylamide Gel Endoribonucleases Enzyme-Linked Immunosorbent Assay Escherichia coli/metabolism Eukaryotic Initiation Factor-4F Eukaryotic Initiation Factor-4G Fungal Proteins/chemistry,metabolism Guanosine Triphosphate/metabolism Ligands Models, Biological Nucleic Acid Conformation Peptide Initiation Factors/chemistry,metabolism Plasmids/metabolism Poly(A)-Binding Proteins Precipitin Tests Protein Binding Protein Biosynthesis Protein Conformation Protein Structure, Tertiary RNA Cap-Binding Proteins RNA, Messenger/metabolism RNA, Ribosomal, 18S/metabolism RNA-Binding Proteins/metabolism Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Time Factors Ultraviolet Rays
Chemicals
Cross-Linking Reagents Eukaryotic Initiation Factor-4F Eukaryotic Initiation Factor-4G Fungal Proteins Ligands Peptide Initiation Factors Poly(A)-Binding Proteins RNA Cap-Binding Proteins RNA, Messenger RNA, Ribosomal, 18S RNA-Binding Proteins Saccharomyces cerevisiae Proteins Guanosine Triphosphate DCP1 protein, S cerevisiae Endoribonucleases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Vilela C
Posttranscriptional Control Group, Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology PO Box 88, Manchester M60 1QD, UK.
Velasco C
Ptushkina M
McCarthy J E
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/19.16.4372
Published
2000-08-15
Pages
4372-82
Language
English
Region
England
NLM ID
8208664
PMCID
PMC302023
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/19.16.4372 PMC Full Text View journal details
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