Protocols for Studying Protein Stability in an Arabidopsis Protoplast Transient Expression System.

Protein stability influences many aspects of biology, and measuring their stability in vivo can provide important insights into biological systems.This chapter describes in detail two methods to assess the stability of a specific protein based on its transient expression in Arabidopsis protoplasts. First, a pulse-chase assay based on radioactive metabolic labeling of cellular proteins, followed by immunoprecipitation of the protein of interest.

Towards plant resistance to viruses using protein-only RNase P.

Plant viruses cause massive crop yield loss worldwide. Most plant viruses are RNA viruses, many of which contain a functional tRNA-like structure. RNase P has the enzymatic activity to catalyze the 5' maturation of precursor tRNAs.

Turnip yellow mosaic virus protease binds ubiquitin suboptimally to fine-tune its deubiquitinase activity.

Single-stranded, positive-sense RNA viruses assemble their replication complexes in infected cells from a multidomain replication polyprotein. This polyprotein usually contains at least one protease, the primary function of which is to process the polyprotein into mature proteins. Such proteases also may have other functions in the replication cycle.

Assembly of gold nanoparticles using turnip yellow mosaic virus as an in-solution SERS sensor.

A common challenge in nanotechnology is the conception of materials with well-defined nanoscale structure. In recent years, virus capsids have been used as templates to create a network to organize 3D nano-objects, building thus new functional nanomaterials and then devices. In this work, we synthetized 3D gold nanoclusters and we used them as Surface Enhanced Raman Scattering (SERS) sensor substrates in solution.

Identification and Molecular Characterization of the Chloroplast Targeting Domain of Replication Proteins.

(TYMV) is a positive-strand RNA virus infecting plants. The TYMV 140K replication protein is a key organizer of viral replication complex (VRC) assembly, being responsible for recruitment of the viral polymerase and for targeting the VRCs to the chloroplast envelope where viral replication takes place. However, the structural requirements determining the subcellular localization and membrane association of this essential viral protein have not yet been defined.