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Molecular chaperones and protein folding in plants

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Abstract

Protein folding in vivo is mediated by an array of proteins that act either as ‘foldases’ or ‘molecular chaperones’. Foldases include protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze the rearrangement of disulfide bonds or isomerization of peptide bonds around Pro residues, respectively. Molecular chaperones are a diverse group of proteins, but they share the property that they bind substrate proteins that are in unstable, non-native structural states. The best understood chaperone systems are HSP70/DnaK and HSP60/GroE, but considerable data support a chaperone role for other proteins, including HSP100, HSP90, small HSPs and calnexin. Recent research indicates that many, if not all, cellular proteins interact with chaperones and/or foldases during their lifetime in the cell. Different chaperone and foldase systems are required for synthesis, targeting, maturation and degradation of proteins in all cellular compartments. Thus, these diverse proteins affect an exceptionally broad array of cellular processes required for both normal cell function and survival of stress conditions. This review summarizes our current understanding of how these proteins function in plants, with a major focus on those systems where the most detailed mechanistic data are available, or where features of the chaperone/foldase system or substrate proteins are unique to plants.

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  1. Department of Botany, North Carolina State University, 27695, Raleigh, NC, USA

    Rebecca S. Boston

  2. Molecular Biology Division, Central Research and Development Department, E.I. DuPont de Nemours and Company, Experimental Station, 19880-0402, Wilmington, DE, USA

    Paul V. Viitanen

  3. Department of Biochemistry, University of Arizona, 85721, Tucson, AZ, USA

    Elizabeth Vierling

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Boston, R.S., Viitanen, P.V. & Vierling, E. Molecular chaperones and protein folding in plants. Plant Mol Biol 32, 191–222 (1996). https://doi.org/10.1007/BF00039383

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