Publication Information
Aguilar-Hernández et al., 2017
No external accession available
Abstract
Mol Plant. 2017 Jun 5;10(6):846-865. doi: 10.1016/j.molp.2017.04.008. Epub 2017
Apr 28.
Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in
Remodeling the Arabidopsis Proteome during Photomorphogenesis.
Aguilar-Hernández V(1), Kim DY(2), Stankey RJ(2), Scalf M(3), Smith LM(3),
Vierstra RD(4).
Author information:
(1)Department of Biology, Washington University in St. Louis, Campus Box 1137,
One Brookings Drive, St. Louis, MO 63130, USA; Department of Genetics, 425-G
Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA.
(2)Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison,
Madison, WI 53706, USA.
(3)Department of Chemistry, 1101 University Avenue, University of
Wisconsin-Madison, Madison, WI 53706, USA.
(4)Department of Biology, Washington University in St. Louis, Campus Box 1137,
One Brookings Drive, St. Louis, MO 63130, USA; Department of Genetics, 425-G
Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA. Electronic
address: rdvierstra@wustl.edu.
The switch from skotomorphogenesis to photomorphogenesis is a key developmental
transition in the life of seed plants. While much of the underpinning proteome
remodeling is driven by light-induced changes in gene expression, the
proteolytic removal of specific proteins by the ubiquitin-26S proteasome system
is also likely paramount. Through mass spectrometric analysis of ubiquitylated
proteins affinity-purified from etiolated Arabidopsis seedlings before and after
red-light irradiation, we identified a number of influential proteins whose
ubiquitylation status is modified during this switch. We observed a
substantial enrichment for proteins involved in auxin, abscisic acid, ethylene,
and brassinosteroid signaling, peroxisome function, disease resistance, protein
phosphorylation and light perception, including the phytochrome (Phy) A and
phototropin photoreceptors. Soon after red-light treatment, PhyA becomes the
dominant ubiquitylated species, with ubiquitin attachment sites mapped to six
lysines. A PhyA mutant protected from ubiquitin addition at these sites is
substantially more stable in planta upon photoconversion to Pfr and is
hyperactive in driving photomorphogenesis. However, light still stimulates
ubiquitylation and degradation of this mutant, implying that other attachment
sites and/or proteolytic pathways exist. Collectively, we expand the catalog of
ubiquitylation targets in Arabidopsis and show that this post-translational
modification is central to the rewiring of plants for photoautotrophic growth.
Copyright © 2017 The Author. Published by Elsevier Inc. All rights reserved.
DOI: 10.1016/j.molp.2017.04.008
PMCID: PMC5695678
PMID: 28461270 [Indexed for MEDLINE]
