skip to main content

DOE PAGESDOE PAGES

Title: E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis

Peroxisomes are ubiquitous eukaryotic organelles that play pivotal roles in a suite of metabolic processes and often act coordinately with other organelles, such as chloroplasts and mitochondria. Peroxisomes import proteins to the peroxisome matrix by peroxins (PEX proteins), but how the function of the PEX proteins is regulated is poorly understood. In this study, we identified the Arabidopsis RING (really interesting new gene) type E3 ubiquitin ligase SP1 [suppressor of plastid protein import locus 1 (ppi1) 1] as a peroxisome membrane protein with a regulatory role in peroxisome protein import. SP1 interacts physically with the two components of the peroxisome protein docking complex PEX13–PEX14 and the (RING)-finger peroxin PEX2. Loss of SP1 function suppresses defects of the pex14-2 and pex13-1 mutants, and SP1 is involved in the degradation of PEX13 and possibly PEX14 and all three RING peroxins. An in vivo ubiquitination assay showed that SP1 has the ability to promote PEX13 ubiquitination. Our study has revealed that, in addition to its previously reported function in chloroplast biogenesis, SP1 plays a role in peroxisome biogenesis. The same E3 ubiquitin ligase promotes the destabilization of components of two distinct protein-import machineries, indicating that degradation of organelle biogenesis factors by the ubiquitin–proteasomemore » system may constitute an important regulatory mechanism in coordinating the biogenesis of metabolically linked organelles in eukaryotes.« less
Authors:
 [1] ;  [1] ; ORCiD logo [2]
  1. Michigan State Univ., East Lansing, MI (United States). Dept. of Energy Plant Research Lab.
  2. Michigan State Univ., East Lansing, MI (United States). Dept. of Energy Plant Research Lab.; Michigan State Univ., East Lansing, MI (United States). Plant Biology Dept.
Publication Date:
Grant/Contract Number:
FG02-91ER20021
Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 113; Journal Issue: 46; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Research Org:
Michigan State Univ., East Lansing, MI (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1330590
Alternate Identifier(s):
OSTI ID: 1465117

Pan, Ronghui, Satkovich, John, and Hu, Jianping. E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis. United States: N. p., Web. doi:10.1073/pnas.1613530113.
Pan, Ronghui, Satkovich, John, & Hu, Jianping. E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis. United States. doi:10.1073/pnas.1613530113.
Pan, Ronghui, Satkovich, John, and Hu, Jianping. 2016. "E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis". United States. doi:10.1073/pnas.1613530113.
@article{osti_1330590,
title = {E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis},
author = {Pan, Ronghui and Satkovich, John and Hu, Jianping},
abstractNote = {Peroxisomes are ubiquitous eukaryotic organelles that play pivotal roles in a suite of metabolic processes and often act coordinately with other organelles, such as chloroplasts and mitochondria. Peroxisomes import proteins to the peroxisome matrix by peroxins (PEX proteins), but how the function of the PEX proteins is regulated is poorly understood. In this study, we identified the Arabidopsis RING (really interesting new gene) type E3 ubiquitin ligase SP1 [suppressor of plastid protein import locus 1 (ppi1) 1] as a peroxisome membrane protein with a regulatory role in peroxisome protein import. SP1 interacts physically with the two components of the peroxisome protein docking complex PEX13–PEX14 and the (RING)-finger peroxin PEX2. Loss of SP1 function suppresses defects of the pex14-2 and pex13-1 mutants, and SP1 is involved in the degradation of PEX13 and possibly PEX14 and all three RING peroxins. An in vivo ubiquitination assay showed that SP1 has the ability to promote PEX13 ubiquitination. Our study has revealed that, in addition to its previously reported function in chloroplast biogenesis, SP1 plays a role in peroxisome biogenesis. The same E3 ubiquitin ligase promotes the destabilization of components of two distinct protein-import machineries, indicating that degradation of organelle biogenesis factors by the ubiquitin–proteasome system may constitute an important regulatory mechanism in coordinating the biogenesis of metabolically linked organelles in eukaryotes.},
doi = {10.1073/pnas.1613530113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 46,
volume = 113,
place = {United States},
year = {2016},
month = {10}
}

Works referenced in this record:

Genome-Wide Insertional Mutagenesis of Arabidopsis thaliana
journal, August 2003
  • Alonso, J. M.; Stepanova, Anna N.; Leisse, Thomas J.
  • Science, Vol. 301, Issue 5633, p. 653-657
  • DOI: 10.1126/science.1086391

Seed Storage Oil Mobilization
journal, June 2008

Enzymatic assembly of DNA molecules up to several hundred kilobases
journal, April 2009
  • Gibson, Daniel G.; Young, Lei; Chuang, Ray-Yuan
  • Nature Methods, Vol. 6, Issue 5, p. 343-345
  • DOI: 10.1038/nmeth.1318

MUSCLE: multiple sequence alignment with high accuracy and high throughput
journal, March 2004
  • Edgar, R. C.
  • Nucleic Acids Research, Vol. 32, Issue 5, p. 1792-1797
  • DOI: 10.1093/nar/gkh340