Formation of ribosome-RNA initiation complexes with alfalfa mosaic virus RNA 4 and RNA 3
Open Access
- 1 January 1979
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 7 (1) , 151-166
- https://doi.org/10.1093/nar/7.1.151
Abstract
RNA 4 of alfalfa mosaic virus (AMV) is a monocistronic messenger for the coat protein. We have determined the sequence of the 40±2 nucleotides in RNA 4 that were protected in the initiation complex formed with wheat germ 80 S ribosomes from digestion by T1 or pancreatic ribonucleases. The AUG coat protein initiation codon was near the middle of this protected region. We have found two ribosome-binding sites in RNA 3. The principal one, near the 5′end, is the initiation site for the major translation product, a 35,000 dalton protein. The second site binds ribosomes only weakly, at the beginning of the “silent” coat protein cistron, and is similar but not identical to the initiation site protected in RNA 4. The possibility of a ribosome-binding at the “silent” cistron initiation site is discussed.Keywords
This publication has 25 references indexed in Scilit:
- How do eucaryotic ribosomes select initiation regions in messenger RNA?Cell, 1978
- Complete sequences of the ribosome recognition sites in vesicular stomatitis virus mRNAs: Recognition by the 40S and 80S complexesCell, 1978
- End labeling of enzymatically decapped mRNANucleic Acids Research, 1977
- The use of nuclease P1in sequence analysis of end group labeled RNANucleic Acids Research, 1977
- Oligonucleotide mapping of picornavirus RNAs by two-dimensional electrophoresisVirology, 1976
- Translation of tobacco rattle virus RNA in vitro using wheat germ extractsVirology, 1976
- Blocked 5' termini in alfalfa mosaic virus RNA.1976
- Translation of alfalfa mosaic virus RNA's in mammalian cell-free systemsVirology, 1975
- Analysis of the Pancreatic-Ribonuclease-Digestion Products of Alfalfa-Mosaic-Virus Ribonucleic Acid. Sequence Homologies between the Different RNAsEuropean Journal of Biochemistry, 1975
- Characterization of a highly efficient protein synthesizing system derived from commercial wheat germNucleic Acids Research, 1974