Ubiquitin-dependent chloroplast-associated protein degradation in plants

Chloroplasts contain thousands of nucleus-encoded proteins that are imported from the cytosol by translocases in the chloroplast envelope membranes. Proteolytic regulation of the translocases is critically important, but little is known about the underlying mechanisms. We applied forward genetics an...

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Vydané v:	Science (American Association for the Advancement of Science) Ročník 363; číslo 6429
Hlavní autori:	Ling, Qihua, Broad, William, Trösch, Raphael, Töpel, Mats, Demiral Sert, Tijen, Lymperopoulos, Panagiotis, Baldwin, Amy, Jarvis, R Paul
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 22.02.2019
Predmet:	Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - metabolism ATPases Associated with Diverse Cellular Activities - metabolism Cell Cycle Proteins - metabolism Chloroplast Proteins Chloroplasts - enzymology Intracellular Signaling Peptides and Proteins - metabolism Membrane Proteins Proteasome Endopeptidase Complex - metabolism Proteolysis Ubiquitin - metabolism Ubiquitin-Protein Ligases - metabolism
ISSN:	1095-9203, 1095-9203
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Shrnutí:	Chloroplasts contain thousands of nucleus-encoded proteins that are imported from the cytosol by translocases in the chloroplast envelope membranes. Proteolytic regulation of the translocases is critically important, but little is known about the underlying mechanisms. We applied forward genetics and proteomics in to identify factors required for chloroplast outer envelope membrane (OEM) protein degradation. We identified SP2, an Omp85-type β-barrel channel of the OEM, and CDC48, a cytosolic AAA+ (ATPase associated with diverse cellular activities) chaperone. Both proteins acted in the same pathway as the ubiquitin E3 ligase SP1, which regulates OEM translocase components. SP2 and CDC48 cooperated to bring about retrotranslocation of ubiquitinated substrates from the OEM (fulfilling conductance and motor functions, respectively), enabling degradation of the substrates by the 26S proteasome in the cytosol. Such chloroplast-associated protein degradation (CHLORAD) is vital for organellar functions and plant development.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1095-9203 1095-9203
DOI:	10.1126/science.aav4467