Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis.

Autor: Aguilar-Hernández V; 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., Kim DY; Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA., Stankey RJ; Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA., Scalf M; Department of Chemistry, 1101 University Avenue, University of Wisconsin-Madison, Madison, WI 53706, USA., Smith LM; Department of Chemistry, 1101 University Avenue, University of Wisconsin-Madison, Madison, WI 53706, USA., Vierstra RD; 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.
Jazyk: angličtina
Zdroj: Molecular plant [Mol Plant] 2017 Jun 05; Vol. 10 (6), pp. 846-865. Date of Electronic Publication: 2017 Apr 28.
DOI: 10.1016/j.molp.2017.04.008
Abstrakt: 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.)
Databáze: MEDLINE
Externí odkaz: