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Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F16%3A00471365" target="_blank" >RIV/61389030:_____/16:00471365 - isvavai.cz</a>

  • Alternative codes found

    RIV/61989592:15310/16:33161734

  • Result on the web

    <a href="http://dx.doi.org/10.3390/plants5010003" target="_blank" >http://dx.doi.org/10.3390/plants5010003</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/plants5010003" target="_blank" >10.3390/plants5010003</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/LO1204" target="_blank" >LO1204: Sustainable development of research in the Centre of the Region Haná</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Plants

  • ISSN

    2223-7747

  • e-ISSN

  • Volume of the periodical

    5

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    11

  • Pages from-to

  • UT code for WoS article

  • EID of the result in the Scopus database

    2-s2.0-85002951384