Dataset Information

Function of clpF in the clp protease complex

ABSTRACT: The plant plastid Clp machinery comprises a hetero-oligomeric ClpPRT proteolytic core, ATP-dependent ClpC,D chaperones and an adaptor protein, ClpS1. ClpS1 directs a subset of substrates to the Clp protease-chaperone complex for degradation, but substrate recognition and delivery mechanisms are unknown. Here we describe ClpF, a novel chloroplast adaptor. ClpF is only found in photosynthetic eukaryotes and contains uvr/C and YccV domains and an N-terminal domain conserved across ClpF homologs. We demonstrate that ClpF acts together with ClpS1 in substrate delivery to plastid ClpC chaperones. The molecular domain interactions of ClpF to ClpS1 and the ClpC chaperones were mapped, and in vivo interactions between ClpF and the Clp substrate glutamate t-RNA reductase (GluTR1) are demonstrated. Quantitative proteomics identified subtle molecular phenotype in a ClpF null mutant and we show that GluTR1 degradation is delayed in ClpF and ClpS1 Arabidopsis null mutants.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Photosynthetic Cell, Leaf

SUBMITTER: Giulia Friso

LAB HEAD: Giulia Friso c/o Klaas van Wijk's Lab

PROVIDER: PXD002186 | Pride | 2019-04-09

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	F063797.dat-pride.pride.mgf.gz	Mgf
	F063797.dat-pride.pride.mztab.gz	Mztab
	F063797.dat-pride.xml.gz	Xml
	F063798.dat-pride.pride.mgf.gz	Mgf
	F063798.dat-pride.pride.mztab.gz	Mztab

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Publications

Discovery of a Unique Clp Component, ClpF, in Chloroplasts: A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery.

Nishimura Kenji K Apitz Janina J Friso Giulia G Kim Jitae J Ponnala Lalit L Grimm Bernhard B van Wijk Klaas J KJ

The Plant cell 20150929 10

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 characteri ...[more]

PMID: 26419670

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