Chloroplast Autophagy and Ubiquitination Combine to Manage Oxidative Damage and Starvation Responses . Issue 4 (17th June 2020)
- Record Type:
- Journal Article
- Title:
- Chloroplast Autophagy and Ubiquitination Combine to Manage Oxidative Damage and Starvation Responses . Issue 4 (17th June 2020)
- Main Title:
- Chloroplast Autophagy and Ubiquitination Combine to Manage Oxidative Damage and Starvation Responses
- Authors:
- Kikuchi, Yuta
Nakamura, Sakuya
Woodson, Jesse D.
Ishida, Hiroyuki
Ling, Qihua
Hidema, Jun
Jarvis, R. Paul
Hagihara, Shinya
Izumi, Masanori - Abstract:
- Abstract : Chloroplast autophagy and chloroplast-associated ubiquitination independently contribute to chloroplast degradation, the management of ROS damage, and the adaptation to starvation. Abstract: Autophagy and the ubiquitin-proteasome system are the major degradation processes for intracellular components in eukaryotes. Although ubiquitination acts as a signal inducing organelle-targeting autophagy, the interaction between ubiquitination and autophagy in chloroplast turnover has not been addressed. In this study, we found that two chloroplast-associated E3 enzymes, SUPPRESSOR OF PPI1 LOCUS1 and PLANT U-BOX4 (PUB4), are not necessary for the induction of either piecemeal autophagy of chloroplast stroma or chlorophagy of whole damaged chloroplasts in Arabidopsis ( Arabidopsis thaliana ). Double mutations of an autophagy gene and PUB4 caused synergistic phenotypes relative to single mutations. The double mutants developed accelerated leaf chlorosis linked to the overaccumulation of reactive oxygen species during senescence and had reduced seed production. Biochemical detection of ubiquitinated proteins indicated that both autophagy and PUB4-associated ubiquitination contributed to protein degradation in the senescing leaves. Furthermore, the double mutants had enhanced susceptibility to carbon or nitrogen starvation relative to single mutants. Together, these results indicate that autophagy and chloroplast-associated E3s cooperate for protein turnover, management ofAbstract : Chloroplast autophagy and chloroplast-associated ubiquitination independently contribute to chloroplast degradation, the management of ROS damage, and the adaptation to starvation. Abstract: Autophagy and the ubiquitin-proteasome system are the major degradation processes for intracellular components in eukaryotes. Although ubiquitination acts as a signal inducing organelle-targeting autophagy, the interaction between ubiquitination and autophagy in chloroplast turnover has not been addressed. In this study, we found that two chloroplast-associated E3 enzymes, SUPPRESSOR OF PPI1 LOCUS1 and PLANT U-BOX4 (PUB4), are not necessary for the induction of either piecemeal autophagy of chloroplast stroma or chlorophagy of whole damaged chloroplasts in Arabidopsis ( Arabidopsis thaliana ). Double mutations of an autophagy gene and PUB4 caused synergistic phenotypes relative to single mutations. The double mutants developed accelerated leaf chlorosis linked to the overaccumulation of reactive oxygen species during senescence and had reduced seed production. Biochemical detection of ubiquitinated proteins indicated that both autophagy and PUB4-associated ubiquitination contributed to protein degradation in the senescing leaves. Furthermore, the double mutants had enhanced susceptibility to carbon or nitrogen starvation relative to single mutants. Together, these results indicate that autophagy and chloroplast-associated E3s cooperate for protein turnover, management of reactive oxygen species accumulation, and adaptation to starvation. … (more)
- Is Part Of:
- Plant physiology. Volume 183:Issue 4(2020)
- Journal:
- Plant physiology
- Issue:
- Volume 183:Issue 4(2020)
- Issue Display:
- Volume 183, Issue 4 (2020)
- Year:
- 2020
- Volume:
- 183
- Issue:
- 4
- Issue Sort Value:
- 2020-0183-0004-0000
- Page Start:
- 1531
- Page End:
- 1544
- Publication Date:
- 2020-06-17
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.20.00237 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16892.xml