Ubiquitin-dependent chloroplast-associated protein degradation in plants

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Ubiquitin-dependent chloroplast-associated protein degradation in plants. / Ling, Qihua; Broad, William; Trösch, Raphael; Töpel, Mats; Sert, Tijen Demiral; Lymperopoulos, Panagiotis; Baldwin, Amy; Jarvis, R. Paul.

In: Science, Vol. 363, No. 6429, eaav4467, 2019.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Ling, Q, Broad, W, Trösch, R, Töpel, M, Sert, TD, Lymperopoulos, P, Baldwin, A & Jarvis, RP 2019, 'Ubiquitin-dependent chloroplast-associated protein degradation in plants', Science, vol. 363, no. 6429, eaav4467. https://doi.org/10.1126/science.aav4467

APA

Ling, Q., Broad, W., Trösch, R., Töpel, M., Sert, T. D., Lymperopoulos, P., Baldwin, A., & Jarvis, R. P. (2019). Ubiquitin-dependent chloroplast-associated protein degradation in plants. Science, 363(6429), [eaav4467]. https://doi.org/10.1126/science.aav4467

Vancouver

Ling Q, Broad W, Trösch R, Töpel M, Sert TD, Lymperopoulos P et al. Ubiquitin-dependent chloroplast-associated protein degradation in plants. Science. 2019;363(6429). eaav4467. https://doi.org/10.1126/science.aav4467

Author

Ling, Qihua ; Broad, William ; Trösch, Raphael ; Töpel, Mats ; Sert, Tijen Demiral ; Lymperopoulos, Panagiotis ; Baldwin, Amy ; Jarvis, R. Paul. / Ubiquitin-dependent chloroplast-associated protein degradation in plants. In: Science. 2019 ; Vol. 363, No. 6429.

Bibtex

@article{945c4b4743124ea6bb42b4c84317ef64,
title = "Ubiquitin-dependent chloroplast-associated protein degradation in plants",
abstract = "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 Arabidopsis 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.",
author = "Qihua Ling and William Broad and Raphael Tr{\"o}sch and Mats T{\"o}pel and Sert, {Tijen Demiral} and Panagiotis Lymperopoulos and Amy Baldwin and Jarvis, {R. Paul}",
year = "2019",
doi = "10.1126/science.aav4467",
language = "English",
volume = "363",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6429",

}

RIS

TY - JOUR

T1 - Ubiquitin-dependent chloroplast-associated protein degradation in plants

AU - Ling, Qihua

AU - Broad, William

AU - Trösch, Raphael

AU - Töpel, Mats

AU - Sert, Tijen Demiral

AU - Lymperopoulos, Panagiotis

AU - Baldwin, Amy

AU - Jarvis, R. Paul

PY - 2019

Y1 - 2019

N2 - 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 Arabidopsis 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.

AB - 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 Arabidopsis 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.

U2 - 10.1126/science.aav4467

DO - 10.1126/science.aav4467

M3 - Journal article

C2 - 30792274

AN - SCOPUS:85061988307

VL - 363

JO - Science

JF - Science

SN - 0036-8075

IS - 6429

M1 - eaav4467

ER -

ID: 223624490