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A Novel Interaction of Cap-binding Protein Complexes Eukaryotic Initiation Factor (eIF) 4F and eIF(iso)4F with a Region in the 3′-Untranslated Region of Satellite Tobacco Necrosis Virus
- Source :
- Journal of Biological Chemistry. 279:13584-13592
- Publication Year :
- 2004
- Publisher :
- Elsevier BV, 2004.
-
Abstract
- Satellite tobacco necrosis virus (STNV) RNA is naturally uncapped at its 5' end and lacks polyadenylation at its 3' end. Despite lacking these two hallmarks of eukaryotic mRNAs, STNV-1 RNA is translated very efficiently. A approximately 130-nucleotide translational enhancer (TED), located 3' to the termination codon, is necessary for efficient cap-independent translation of STNV-1 RNA. The STNV-1 TED RNA fragment binds to the eukaryotic cap-binding complexes, initiation factor (eIF) 4F and eIF(iso)4F, as measured by nitrocellulose binding and fluorescence titration. STNV-1 TED is a potent inhibitor of in vitro translation when added in trans. This inhibition is reversed by the addition of eIF4F or eIF(iso)4F, and the subunits of eIF4F and eIF(iso)4F cross-link to STNV-1 TED, providing additional evidence that these factors interact directly with STNV-1 TED. Deletion mutagenesis of the STNV-1 TED indicates that a minimal region of approximately 100 nucleotides is necessary to promote cap-independent translation primarily through interaction with the cap binding subunits (eIF4E or eIF(iso)4E) of eIF4F or eIF(iso)4F.
- Subjects :
- Polyadenylation
Ultraviolet Rays
Molecular Sequence Data
Biology
Biochemistry
Eukaryotic initiation factor 4F
Two-Hybrid System Techniques
Eukaryotic initiation factor
Protein biosynthesis
Initiation factor
3' Untranslated Regions
Molecular Biology
Base Sequence
Three prime untranslated region
EIF4E
RNA
Cell Biology
Precipitin Tests
Molecular biology
Eukaryotic Initiation Factor-4F
Mutagenesis
Protein Biosynthesis
Nucleic Acid Conformation
RNA, Viral
Tobacco necrosis satellite virus
Ribosomes
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 279
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....c8f0a11a5fe1de87942a93d5df332293