The eIF1A Solution Structure Reveals a Large RNA-Binding Surface Important for Scanning Function
Copyright policy )The eIF1A Solution Structure Reveals a Large RNA-Binding Surface Important for Scanning Function
The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.
- Lomonosov Moscow State University Russian Federation
- Harvard University United States
- State University of New York United States
- State University of New York at Potsdam United States
Models, Molecular, Protein Folding, Binding Sites, Oligoribonucleotides, Bacteria, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Eukaryotic Initiation Factor-1, Cell Biology, Saccharomyces cerevisiae, Archaea, Protein Structure, Secondary, Recombinant Proteins, Peptide Initiation Factors, Humans, Amino Acid Sequence, RNA, Messenger, Codon, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment
Models, Molecular, Protein Folding, Binding Sites, Oligoribonucleotides, Bacteria, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Eukaryotic Initiation Factor-1, Cell Biology, Saccharomyces cerevisiae, Archaea, Protein Structure, Secondary, Recombinant Proteins, Peptide Initiation Factors, Humans, Amino Acid Sequence, RNA, Messenger, Codon, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment
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