Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions.

Autor:	Torres-Romero D; Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain., Gómez-Zambrano Á; Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain., Serrato AJ; Estación Experimental del Zaidín, CSIC, Calle Profesor Albareda 1, 18008 Granada, Spain., Sahrawy M; Estación Experimental del Zaidín, CSIC, Calle Profesor Albareda 1, 18008 Granada, Spain., Mérida Á; Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain.
Jazyk:	angličtina
Zdroj:	Journal of experimental botany [J Exp Bot] 2022 Jan 27; Vol. 73 (3), pp. 903-914.
DOI:	10.1093/jxb/erab452
Abstrakt:	Fibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2. We show that these three polypeptides interact between each other, potentially forming a network around the plastoglobule surface. Both FBN2 and FBN1s interact with allene oxide synthase, and the elimination of any of these FBNs results in a delay in jasmonate-mediated anthocyanin accumulation in response to a combination of moderate high light and low temperature. Mutations in the genes encoding FBN1s or FBN2 also affect the protection of PSII under the combination of these stresses. Fully developed leaves of these mutants have lower maximum quantum efficiency of PSII (Fv/Fm) and higher oxidative stress than wild-type plants. These effects are additive, and the fbn1a-1b-2 triple mutant shows a stronger decrease in Fv/Fm and a greater increase in oxidative stress than fbn1a-1b or fbn2 mutants. Co-immunoprecipitation analysis indicated that FBN2 also interacts with other proteins involved in different metabolic processes. We propose that these fibrillins facilitate accurate positioning of different proteins involved in distinct metabolic processes, and that their elimination leads to dysfunction of those proteins. (© The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology.)
Databáze:	MEDLINE
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