Characterization of ubiquitin ligase SlATL31 and proteomic analysis of 14-3-3 targets in tomato fruit tissue (Solanum lycopersicum L.).
The 14-3-3 proteins participate in many aspects of plant physiology by interacting with phosphorylated proteins and thereby regulating target protein functions. In Arabidopsis plant, the ubiquitin ligase ATL31 controls 14-3-3 stability via both direct interaction and ubiquitination, and this consequently regulates post-germinative growth in response to carbon and nitrogen nutrient availability. Since 14-3-3 proteins regulate the activities of many key enzymes related to nutrient metabolism, one would anticipate that they should play an essential role not only in vegetative but also in reproductive tissue. Because fruit yield largely depends on carbon and nitrogen availability and their utilization, the function of 14-3-3 proteins was analyzed in tomato fruit tissue. Here, we isolated and characterized an ubiquitin ligase SlATL31 (Solyc03g112340) from tomato and demonstrated that SlATL31 has ubiquitin ligase activity as well as interaction with tomato 14-3-3 proteins, suggesting the possibility that the SlATL31 functions as an ubiquitin ligase for 14-3-3 similarly to its Arabidopsis ortholog. Furthermore, we performed proteomic analysis of 14-3-3 interacting proteins and identified 106 proteins as putative 14-3-3 targets including key enzymes for carbon metabolism and photosynthesis. This 14-3-3 interactome result and available transcriptome profile suggest a considerable yet complex role of 14-3-3 proteins in tomato fruit tissue.



Considerable cumulative evidence exists which implies that 14-3-3 proteins are involved in the regulation of plant primary metabolism. Here we provide the first report of 14-3-3 interactome analysis and identify putative 14-3-3 targets in tomato fruit tissue, which may be highly important given the documented metabolic shifts, which occur during fruit development and ripening. These data open future research avenues by which to understand the regulation of the role of post-translational regulation in tomato fruit development.
Faculty of Science and Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan. Electronic address: luyu0120@mail.sci.hokudai.ac.jp.
Yu
Y
Lu
Faculty of Science and Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan. Electronic address: antian.shengui@mail.sci.hokudai.ac.jp.
Shigetaka
S
Yasuda
Faculty of Science and Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan. Electronic address: lixingwen1214@mail.sci.hokudai.ac.jp.
Xingwen
X
Li
Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan. Electronic address: y-fukao@fc.ritsumei.ac.jp.
Yoichiro
Y
Fukao
Max-Planck-Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476 Potsdam-Golm, Germany. Electronic address: tohge@mpimp-golm.mpg.de.
Takayuki
T
Tohge
Max-Planck-Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476 Potsdam-Golm, Germany. Electronic address: fernie@mpimp-golm.mpg.de.
Alisdair R
AR
Fernie
Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba 305-8572, Japan. Electronic address: matsukura.chiaki.fw@u.tsukuba.ac.jp.
Chiaki
C
Matsukura
Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba 305-8572, Japan. Electronic address: ezura@gene.tsukuba.ac.jp.
Hiroshi
H
Ezura
Faculty of Science and Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan. Electronic address: t-satou@sci.hokudai.ac.jp.
Takeo
T
Sato
Faculty of Science and Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan. Electronic address: jjyama@sci.hokudai.ac.jp.
Junji
J
Yamaguchi
D048948:14-3-3 Proteins / Q000378:metabolism / Q000502:physiology*; D002244:Carbon / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D018551:Solanum lycopersicum / Q000737:chemistry* / Q000201:enzymology; D009584:Nitrogen / Q000378:metabolism; D010940:Plant Proteins / Q000032:analysis / Q000378:metabolism* / Q000502:physiology; D060066:Protein Interaction Maps; D040901:Proteomics / Q000379:methods*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D048948:14-3-3 Proteins; D010940:Plant Proteins; D002244:Carbon; D044767:Ubiquitin-Protein Ligases; C000624844:ubiquitin ligase SlATL31, tomato; D009584:Nitrogen
14-3-3 protein; Carbon metabolism; Fruit; Protein interactome; Tomato; Ubiquitin ligase