Abstract
The eukaryotic mRNA 5' cap structure m7GpppX (where X is any nucleotide) interacts with a number of cellular proteins. Several of these proteins were studied in mammalian, yeast, and drosophila cells and found to be involved in translation initiation. Here we describe a novel cap-binding protein, the coat protein of L-A, a double-stranded RNA virus that is persistently maintained in many Saccharomyces cerevisiae strains. The results also suggest that the coat protein of a related double-stranded RNA virus (L-BC) is likewise a cap-binding protein. Strikingly, in contrast to the cellular cap-binding proteins, the interaction between the L-A virus coat protein and the cap structure is through a covalent bond.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Binding Sites
-
Capsid / genetics
-
Capsid / isolation & purification
-
Capsid / metabolism*
-
Cyanogen Bromide
-
Genotype
-
Kinetics
-
Molecular Sequence Data
-
Peptide Fragments / isolation & purification
-
RNA Caps / metabolism*
-
RNA Viruses / genetics
-
RNA Viruses / metabolism*
-
RNA, Double-Stranded / genetics
-
RNA, Messenger / metabolism*
-
Ribonucleases
-
Ribosomes / metabolism
-
Saccharomyces cerevisiae / genetics
-
Saccharomyces cerevisiae / metabolism*
-
Sequence Homology, Nucleic Acid
-
Thermodynamics
-
Transcription, Genetic
-
Trypsin
Substances
-
Peptide Fragments
-
RNA Caps
-
RNA, Double-Stranded
-
RNA, Messenger
-
Ribonucleases
-
Trypsin
-
Cyanogen Bromide