title: ATP-dependent molecular chaperones in plastids--More complex than expected.
abstract: Plastids are a class of essential plant cell organelles comprising photosynthetic chloroplasts of green tissues, starch-storing amyloplasts of roots and tubers or the colorful pigment-storing chromoplasts of petals and fruits. They express a few genes encoded on their organellar genome, called plastome, but import most of their proteins from the cytosol. The import into plastids, the folding of freshly-translated or imported proteins, the degradation or renaturation of denatured and entangled proteins, and the quality-control of newly folded proteins all require the action of molecular chaperones. Members of all four major families of ATP-dependent molecular chaperones (chaperonin/Cpn60, Hsp70, Hsp90 and Hsp100 families) have been identified in plastids from unicellular algae to higher plants. This review aims not only at giving an overview of the most current insights into the general and conserved functions of these plastid chaperones, but also into their specific plastid functions. Given that chloroplasts harbor an extreme environment that cycles between reduced and oxidized states, that has to deal with reactive oxygen species and is highly reactive to environmental and developmental signals, it can be presumed that plastid chaperones have evolved a plethora of specific functions some of which are just about to be discovered. Here, the most urgent questions that remain unsolved are discussed, and guidance for future research on plastid chaperones is given. This article is part of a Special Issue entitled: Chloroplast Biogenesis.
authors.affiliation: TU Kaiserslautern, Molecular Biotechnology & Systems Biology, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany; HU Berlin, Institute of Biology, Chausseestraße 117, 10115 Berlin, Germany; TU Kaiserslautern, Molecular Genetics of Eukaryotes, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany. Electronic address: raphael.troesch@aol.de.
authors.forename: Raphael
authors.initials: R
authors.lastname: Trösch
authors.affiliation: TU Kaiserslautern, Molecular Biotechnology & Systems Biology, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany. Electronic address: muehlhaus@bio.uni-kl.de.
authors.forename: Timo
authors.initials: T
authors.lastname: Mühlhaus
authors.affiliation: TU Kaiserslautern, Molecular Biotechnology & Systems Biology, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany. Electronic address: schroda@bio.uni-kl.de.
authors.forename: Michael
authors.initials: M
authors.lastname: Schroda
authors.affiliation: TU Kaiserslautern, Molecular Genetics of Eukaryotes, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany. Electronic address: willmund@bio.uni-kl.de.
authors.forename: Felix
authors.initials: F
authors.lastname: Willmund
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D018832:Molecular Chaperones / Q000502:physiology*; D010084:Oxidation-Reduction; D018087:Plastids / Q000502:physiology*; D017510:Protein Folding; D021381:Protein Transport
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate
keywords: Abiotic stress; Molecular chaperone; Photosynthesis; Plastid development; Protein folding; Protein homeostasis