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Arabidopsis FTSH11 mutant

ABSTRACT: The membrane-integrated metallo-protease FtsH11 of Arabidopsis thaliana is proposed to be dual targeted to mitochondria and chloroplasts. A bleached phenotype was observed in ftsh11 grown at long days or continuous light, pointing to disturbances in the chloroplast. Under these growth conditions the morphology of the chloroplast became drastically altered, accompanied by a drop of NPQ, and the amount of PSI decreased relative to PSII. The abundance of plastidic proteins, especially of photosynthetic proteins, was altered in ftsh11 even during growth in normal conditions and short days. FtsH11 is crucial for chloroplast structure and function during growth in prolonged photoperiod . In chloroplasts FtsH11 was found to be located exclusively in the chloroplast envelope. Thanks to proteomic analyses, the Tic22-like protein and YGGT, both chloroplast proteins of unknown function, are proposed to be the substrates of FtsH11 .

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Sabine Brugiere

LAB HEAD: ferro

PROVIDER: PXD002969 | Pride | 2022-03-03

REPOSITORIES: Pride

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Project description:Chloroplast is a major plant cell organelle that fulfills essential metabolic and biosynthetic functions. Located at the interface between the chloroplast and other cell compartments, the chloroplast envelope system is a strategic barrier controlling exchanges of ions, metabolites and proteins, thus regulating essential metabolic functions (synthesis of hormones precursors, amino acids, pigments, sugars, vitamins, lipids, nucleotides…) of the plant cell. However, chloroplast envelope membranes remain the hidden part of the chloroplast proteome and many envelope proteins remain to be characterized (known but uncharacterized envelope proteins) or identified (orphan known envelope-associated functions carried by unidentified proteins) Indeed, the envelope contains only 1% of the chloroplast proteins (i.e. 0.25% of the whole cell proteome). When comparing the composition crude leaf extract and purified envelope vesicles, a high theoretical enrichment factor (EF) of specific envelope proteins is thus expected. This is especially true for minor envelope proteins (e.g. representing 1/100 or 1/1000 of the envelope protein content). Sensitivity of MS technique has been greatly improved during the last decade. Today, thanks to the continuous improvement of MS techniques, we are able to detect more components in a complex sample, to generate quantitative data and to statistically validate above-cited enrichment factor. Here, we have taken advantage of present-days better MS sensitivity towards a better definition (differentiate genuine envelope proteins from contaminants) of the chloroplast envelope proteome. This MS- and statistical-based analysis relied on an enrichment factor calculated for each protein identified in purified envelope fractions when compared to the value obtained for the same protein in crude cell extracts. Using this approach, a total of 1376 proteins was detected in purified envelope fractions, of which, more than 500 could be assigned an envelope localization combining MS-based statistical analyses and manual annotation using data from the literature or prediction tools. Interestingly, many of such proteins being unknown or unexpected envelope components, these data constitute a new resource of significant value to the broader plant science community aiming to define principles and molecular mechanisms controlling fundamental aspects of plastid biogenesis and functions.

			Action	DRS
	FUNK_samples_Pride.xlsx	Xlsx
	VELOS11771.raw	Raw
	VELOS11772.raw	Raw
	VELOS11773.raw	Raw
	VELOS11776.raw	Raw

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Arabidopsis FTSH11 mutant

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