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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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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Project description:Plastids contain multiple copies of the plastid chromosome, folded together with proteins and RNA into nucleoids. The degree to which components of the plastid gene expression and protein biogenesis machineries are nucleoid associated, and the factors involved in plastid DNA organization, repair, and replication, are poorly understood. To provide a conceptual framework for nucleoid function, we characterized the proteomes of highly enriched nucleoid fractions of proplastids and mature chloroplasts isolated from the maize (Zea mays) leaf base and tip, respectively, using mass spectrometry. Quantitative comparisons with proteomes of unfractionated proplastids and chloroplasts facilitated the determination of nucleoid-enriched proteins. This nucleoid-enriched proteome included proteins involved in DNA replication, organization, and repair as well as transcription, mRNA processing, splicing, and editing. Many proteins of unknown function, including pentatricopeptide repeat (PPR), tetratricopeptide repeat (TPR), DnaJ, and mitochondrial transcription factor (mTERF) domain proteins, were identified. Strikingly, 70S ribosome and ribosome assembly factors were strongly overrepresented in nucleoid fractions, but protein chaperones were not. Our analysis strongly suggests that mRNA processing, splicing, and editing, as well as ribosome assembly, take place in association with the nucleoid, suggesting that these processes occur cotranscriptionally. The plastid developmental state did not dramatically change the nucleoid-enriched proteome but did quantitatively shift the predominating function from RNA metabolism in undeveloped plastids to translation and homeostasis in chloroplasts. This study extends the known maize plastid proteome by hundreds of proteins, including more than 40 PPR and mTERF domain proteins, and provides a resource for targeted studies on plastid gene expression. Details of protein identification and annotation are provided in the Plant Proteome Database.

Dataset Information

Function of clpF in the clp protease complex

Publications

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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