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Plants 2016, 5(1), 3; doi:10.3390/plants5010003

Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members

1
Department of Cell and Metabolic Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany
2
Department of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany
3
Department of Natural Product Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany
4
Laboratory of Growth Regulators, Centre of the Region Haná for Biotechnological and Agricultural Research, Institute of Experimental Botany AS CR & Palacký University, Šlechtitelů 11, CZ-78371 Olomouc, Czech Republic
*
Author to whom correspondence should be addressed.
Academic Editor: Debora Gasperini
Received: 20 November 2015 / Revised: 22 December 2015 / Accepted: 29 December 2015 / Published: 6 January 2016
(This article belongs to the Special Issue The Jasmonate Pathway)
View Full-Text   |   Download PDF [1965 KB, uploaded 6 January 2016]   |  

Abstract

Jasmonates (JAs) are lipid-derived signals in plant stress responses and development. A crucial step in JA biosynthesis is catalyzed by allene oxide cyclase (AOC). Four genes encoding functional AOCs (AOC1, AOC2, AOC3 and AOC4) have been characterized for Arabidopsis thaliana in terms of organ- and tissue-specific expression, mutant phenotypes, promoter activities and initial in vivo protein interaction studies suggesting functional redundancy and diversification, including first hints at enzyme activity control by protein-protein interaction. Here, these analyses were extended by detailed analysis of recombinant proteins produced in Escherichia coli. Treatment of purified AOC2 with SDS at different temperatures, chemical cross-linking experiments and protein structure analysis by molecular modelling approaches were performed. Several salt bridges between monomers and a hydrophobic core within the AOC2 trimer were identified and functionally proven by site-directed mutagenesis. The data obtained showed that AOC2 acts as a trimer. Finally, AOC activity was determined in heteromers formed by pairwise combinations of the four AOC isoforms. The highest activities were found for heteromers containing AOC4 + AOC1 and AOC4 + AOC2, respectively. All data are in line with an enzyme activity control of all four AOCs by heteromerization, thereby supporting a putative fine-tuning in JA formation by various regulatory principles. View Full-Text
Keywords: Arabidopsis allene oxide cyclase isoforms; heteromerization; protein structure analysis; site-directed mutagenesis; activity regulation Arabidopsis allene oxide cyclase isoforms; heteromerization; protein structure analysis; site-directed mutagenesis; activity regulation
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Otto, M.; Naumann, C.; Brandt, W.; Wasternack, C.; Hause, B. Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members. Plants 2016, 5, 3.

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