RNA-protein interactions in the assembly of tobacco mosaic virus
Assembly of tobacco mosaic virus is initiated by the binding of a specific loop of the RNA into the central hole of the disk aggregate of protein subunits. Since the nucleation loop is located about five-sixths along the RNA molecule, subsequent elongation must be bidirectional. We have now measured the rates of elongation in the two directions by determining the lengths of RNA protected from nuclease digestion at different times and using either intact TMV RNA, or RNA with most of the longer tail removed. Comparison of the rates with the protein supplied as either a mixture of disks with A-protein (a mixture of less aggregated states) or just A-protein, shows that different mechanisms and protein aggregates are used for the most rapid growth. When the disks are present, they add more rapidly along the longer RNA tail but do not appear to add directly on the shorter tail. In contrast, smaller aggregates (A-protein) can add at both ends of the rod, but do so more slowly. Mechanisms for these processes are discussed. Preliminary results on the binding of the specific hexanucleotide AAGAAG to the disk are given and compared with the known changes on binding nonspecific hexanucleotides or the trinucleotide AAG.
- Research Organization:
- Medical Research Council, Cambridge, England
- OSTI ID:
- 6856880
- Journal Information:
- Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550700 -- Microbiology
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59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL PATHWAYS
ENZYMES
ESTERASES
HYDROLASES
KINETICS
MICROORGANISMS
MOLECULAR STRUCTURE
MORPHOLOGY
NUCLEATION
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PHOSPHODIESTERASES
REACTION KINETICS
RECEPTORS
RNA
RNA-ASE
STRUCTURAL CHEMICAL ANALYSIS
TOBACCO MOSAIC VIRUS
VIRUSES