title: Organization, function and substrates of the essential Clp protease system in plastids.
abstract: Intra-plastid proteolysis is essential in plastid biogenesis, differentiation and plastid protein homeostasis (proteostasis). We provide a comprehensive review of the Clp protease system present in all plastid types and we draw lessons from structural and functional information of bacterial Clp systems. The Clp system plays a central role in plastid development and function, through selective removal of miss-folded, aggregated, or otherwise unwanted proteins. The Clp system consists of a tetradecameric proteolytic core with catalytically active ClpP and inactive ClpR subunits, hexameric ATP-dependent chaperones (ClpC,D) and adaptor protein(s) (ClpS1) enhancing delivery of subsets of substrates. Many structural and functional features of the plastid Clp system are now understood though extensive reverse genetics analysis combined with biochemical analysis, as well as large scale quantitative proteomics for loss-of-function mutants of Clp core, chaperone and ClpS1 subunits. Evolutionary diversification of Clp system across non-photosynthetic and photosynthetic prokaryotes and organelles is illustrated. Multiple substrates have been suggested based on their direct interaction with the ClpS1 adaptor or screening of different loss-of-function protease mutants. The main challenge is now to determine degradation signals (degrons) in Clp substrates and substrate delivery mechanisms, as well as functional interactions of Clp with other plastid proteases. This article is part of a Special Issue entitled: Chloroplast Biogenesis.
authors.affiliation: Department of Plant Biology, Cornell University, Ithaca, New York 14853.
authors.forename: Kenji
authors.initials: K
authors.lastname: Nishimura
authors.affiliation: Department of Plant Biology, Cornell University, Ithaca, New York 14853. Electronic address: kv35@cornell.edu.
authors.forename: Klaas J
authors.initials: KJ
authors.lastname: van Wijk
mesh_terms: D049071:Endopeptidase Clp / Q000737:chemistry / Q000502:physiology*; D004795:Enzyme Stability; D019143:Evolution, Molecular; D018087:Plastids / Q000378:metabolism*; D059748:Proteolysis; D020543:Proteome
chemical_list: D020543:Proteome; D049071:Endopeptidase Clp
keywords: Clp protease; N-end rule; chloroplast; proteostasis