A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

FEBS Letters

Kust, S.V.¹  Orlov, V.N.¹  Dobrov, E.N.¹  Drachev, V.A.¹  Kalmykov, P.V.¹  Krivosheev, V.P.¹ 

[1] A. N. Belozersky Institute of Physical and Chemical Biology, Moscow State University, Moscow 119899, Russia

关键词: Ordered aggregation;    ts mutation;    Differential scanning calorimetry;    Thermal stability;    Tobacco mosaic virus;    Coat protein;    TMV;    tobacco mosaic virus;    CP;    coat protein;    RP;    repoymerized protein;    DSC;    differential scanning calorimetry;    PB;    phosphate buffer;   

DOI  :  10.1016/S0014-5793(98)00924-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The differential scanning calorimetry (DSC) ‘melting curves’ for virions and coat proteins (CP) of wild-type tobacco mosaic virus (strain U1) and for its CP ts mutant ts21–66 were measured. Strain U1 and ts21–66 mutant (two amino acid substitutions in CP: I21 → T and D66 → G) differ in the type of symptoms they induce on some host plants. It was observed that CP subunits of both U1 and ts21–66 at pH 8.0, in the form of small (3–4S) aggregates, possess much lower thermal stability than in the virions. Assembly into the virus particles resulted in a DSC melting temperature increase from 41 to 72°C for U1 and from 38 to 72°C for ts21–66 CP. In the RNA-free helical virus-like protein assemblies U1 and ts21–66 CP subunits had a thermal stability intermediate between those in 3–4S aggregates and in the virions. ts21–66 helical protein displayed a somewhat lower thermal stability than U1.

【 授权许可】

Unknown