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PMID: 8980480 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Molecular chaperones and protein folding in plants.

Plant molecular biology ·Vol. 32 ·No. 1-2 ·1996-10-00 ·Pages 191-222

Boston RS, Viitanen PV, Vierling E

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.

MeSH Terms
Molecular Chaperones/metabolism Plants/enzymology,metabolism Protein Folding Subcellular Fractions/enzymology,metabolism
Chemicals
Molecular Chaperones
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Boston R S
Department of Botany, North Carolina State University, Raleigh 27695, USA.
Viitanen P V
Vierling E
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Article Info
Journal
Plant molecular biology
Abbr.
Plant Mol Biol
ISSN
0167-4412
DOI
10.1007/BF00039383
Published
1996-10-00
Pages
191-222
Language
English
Region
Netherlands
NLM ID
9106343
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00039383 View journal details
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