Misfolded plant virus proteins: elicitors and targets of ubiquitylation

FEBS Letters

Wiegand, Christiane¹  Jockusch, Harald¹ 

[1] Developmental Biology and Molecular Pathology, Bielefeld University, W7, 33501 Bielefeld, Germany

关键词: Tobacco mosaic virus;    Ubiquitin;    Coat protein;    Temperature-sensitive mutation;    Denaturation;    Insoluble protein;   

DOI  :  10.1016/S0014-5793(03)00549-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mutant tobacco mosaic virus (TMV) coat proteins (CPs) with known amino acid replacements provide well defined examples of destabilized tertiary structures. Here we show that misfolded TMV CPs, but not functional wild-type CPs, induce massive ubiquitylation in tobacco cells and that denatured, insoluble CP subunits are the main substrates of ubiquitin conjugation. As TMV CPs can be easily manipulated they are unique tools to study the molecular basis of the plant cell's response to aberrant protein structures and the associated intracellular stress reactions.

【 授权许可】

Unknown