Studies on the mechanism of assembly of tobacco mosaic virus
Sedimentation and proton binding studies of the endothermic self-association of tobacco mosaic virus (TMV) protein indicate that the so-called 20S sedimenting protein is an interaction system involving at least the 34-subunit two-turn cylindrical disk aggregate and the 49-subunit three-turn helical rod. The pH dependence of this overall equilibrium suggests that disk formation is proton-linked through the binding of protons to the two-turn helix which is not present at significant concentrations near pH 7. There is a temperature-induced intramolecular conformation change in the protein leading to a difference spectrum which is complete in 5 x 10/sup -6/s at pH 7 and 20/sup 0/C and is dominated at 300 nm by tryptophan residues. The probable binding frame at the internal assembly nucleation site of TMV-RNA has been determined by measuring the association constants for the binding of various trinucleoside diphosphates to helical TMV protein rods. The -CAG-AAG-AAG-sequence at the nucleation site is capable of providing at least 10 to 14 kcal/mol of sites of binding free energy for the nucleation event in TMV self-assembly.
- Research Organization:
- Univ. of Connecticut, Storrs
- OSTI ID:
- 6796052
- 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
550800 -- Morphology
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
DYNAMIC FUNCTION STUDIES
KINETICS
MICROORGANISMS
MOLECULAR STRUCTURE
MORPHOLOGICAL CHANGES
MORPHOLOGY
NUCLEATION
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PH VALUE
REACTION KINETICS
RNA
TOBACCO MOSAIC VIRUS
ULTRASTRUCTURAL CHANGES
VIRUSES