Dataset Information

Proteomic analysis of WT, gun1-101, clpc1 and gun1clpc1

ABSTRACT: To understand the differences of the wild type, gun1, clpc1 and gun1clpc1 on the proteome level.

INSTRUMENT(S): Q Exactive

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

TISSUE(S): Plant Cell, Whole Body

SUBMITTER: Guo-Zhang Wu

LAB HEAD: Ralph Bock

PROVIDER: PXD010730 | Pride | 2019-04-23

REPOSITORIES: Pride

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Publications

Control of retrograde signalling by protein import and cytosolic folding stress.

Wu Guo-Zhang GZ Meyer Etienne H EH Richter Andreas S AS Schuster Maja M Ling Qihua Q Schöttler Mark A MA Walther Dirk D Zoschke Reimo R Grimm Bernhard B Jarvis R Paul RP Bock Ralph R

Nature plants 20190506 5

Communication between organelles and the nucleus is essential for fitness and survival. Retrograde signals are cues emitted from the organelles to regulate nuclear gene expression. GENOMES UNCOUPLED1 (GUN1), a protein of unknown function, has emerged as a central integrator, participating in multiple retrograde signalling pathways that collectively regulate the nuclear transcriptome. Here, we show that GUN1 regulates chloroplast protein import through interaction with the import-related chaperon ...[more]

PMID: 31061535

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Project description:In chloroplasts, homeostasis of the proteome maintained by protein synthesis, importation, and degradation is critical to the development of chloroplasts. The caseinolytic protease complex component CLPC1, a member of the HSP100 family of chaperones, not only facilitates the translocation of pre-proteins into chloroplasts, but also mediates protein degradation via its associated caseinolytic protease complex (CLPPs). Although CLPC1 has been shown to affect the abundance of some chloroplast proteins, its overall functions and coordination with other protease systems in maintaining proteome homeostasis have not been fully elucidated. Its possible roles in gene expression are also unclear. Here we used the iTRAQ technique to profile the chloroplast proteomes of the clpc1 mutant and its various complementation lines. Whereas proteins involved in photosynthesis were found to be dramatically decreased in the clcp1 mutant, many involved in chloroplast transcription and translation were increased. Expression of the full-length CLPC1 protein, but not of the N-terminal truncated form (ΔN), in clpc1 restored the level of most of these proteins to that of the wild type. Interestingly, the ΔN complementation line could also restore certain proteins to the wild type level. We found that nearly half of previously suggested candidate substrates of the CLPS1, another CLPP component, were mis-regulated in clpc1, indicating that CLPC1 greatly affects CLPS1 targets. We provide the first experimental evidence to show that CLPC1 profoundly affects gene transcription in chloroplasts. Sense transcripts of many chloroplast genes are up-regulated whereas antisense transcripts down-regulated in the clpc1 mutant. We propose that this altered transcript landscape is a result of the transcription and degradation dynamics conditioned by the changed proteomic profile in the mutant. Our study reveals that CLPC1 and likely the CLPP proteasome complex have a greater than previously recognized role in coordinating and maintaining the proteome and transcriptome homeostasis in chloroplasts.

			Action	DRS
	GZ01-Col-rep1.raw	Raw
	GZ02-gun1-rep1.raw	Raw
	GZ03-clpc1-rep1.raw	Raw
	GZ05-gun1clpc1-rep1.raw	Raw
	GZ07-Col-rep2.raw	Raw