Nishimura, Kenji;
Apitz, Janina;
Friso, Giulia;
Kim, Jitae;
Ponnala, Lalit;
Grimm, Bernhard;
van Wijk, Klaas J.
Discovery of a Unique Clp Component, ClpF, in Chloroplasts: : A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery
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Medientyp:
E-Artikel
Titel:
Discovery of a Unique Clp Component, ClpF, in Chloroplasts: : A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery
Beteiligte:
Nishimura, Kenji;
Apitz, Janina;
Friso, Giulia;
Kim, Jitae;
Ponnala, Lalit;
Grimm, Bernhard;
van Wijk, Klaas J.
Erschienen:
American Society of Plant Biologists, 2015
Beschreibung:
<p>Clp proteases are found in prokaryotes, mitochondria, and plastids where they play crucial roles in maintaining protein homeostasis (proteostasis). The plant plastid Clp machinery comprises a hetero-oligomeric ClpPRT proteolytic core, ATP-dependent chaperones ClpC and ClpD, and an adaptor protein, ClpS1. ClpS1 selects substrates to the ClpPR protease-ClpC chaperone complex for degradation, but the underlying substrate recognition and delivery mechanisms are currently unclear. Here, we characterize a ClpS1-interacting protein in <italic>Arabidopsis thaliana</italic>, ClpF, which can interact with the Clp substrate glutamyl-tRNA reductase. ClpF and ClpS1 mutually stimulate their association with ClpC. ClpF, which is only found in photosynthetic eukaryotes, contains bacterial uvrB/C and YccV protein domains and a unique N-terminal domain. We propose a testable model in which ClpS1 and ClpF form a binary adaptor for selective substrate recognition and delivery to ClpC, reflecting an evolutionary adaptation of the Clp system to the plastid proteome.</p>