ISSN:
1573-4943
Keywords:
Tobacco mosaic virus coat protein
;
ts mutations
;
partial denaturation
;
ordered aggregation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Amino acid substitutions in a majority of tobacco mosaic virus (TMV) coat protein (CP) ts-mutants have previously been mapped to the same region of the CP molecule tertiary structure, located at a distance of about 70 Å from TMV virion axis. In the present work some properties of a new TMV CP ts-mutant ts21-66 (two substitutions I21 ⇒ T and D66 ⇒ G, both in the 70-Å region) were studied. Thermal inactivation characteristics, sedimentation properties, circular dichroism spectra, and modification by a lysine-specific reagent, trinitrobenzensulfonic acid, of ts21–66 CP were compared with those of wild-type (U1) TMV CP. It is concluded that the 70-Å region represents the most labile portion of the TMV CP molecule. Partial disordering of this region in the mutant CP at permissive temperatures leads to loss of the capacity to form two-layer aggregates of the cylindrical type, while further disordering induced by mild heating results also in the loss of the ability to form ordered helical aggregates.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1026338827266
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