Plant auto-inhibited Ca2+-ATPases (ACA) are crucial in defining the shape of calcium transients and therefore in eliciting plant responses to various stimuli. Arabidopsis thaliana genome encodes ten ACA isoforms that can be divided into four clusters based on gene structure and sequence homology. While isoforms from clusters 1, 2 and 4 have been characterized, virtually nothing is known about members of cluster 3 (ACA12 and ACA13). Here we show that a GFP-tagged ACA12 localizes at the plasma membrane and that expression of ACA12 rescues the phenotype of partial male sterility of a null mutant of the plasma membrane isoform ACA9, thus providing genetic evidence that ACA12 is a functional plasma membrane-resident Ca2+-ATPase. By ACA12 expression in yeast and purification by CaM-affinity chromatography, we show that, unlike other ACAs, the activity of ACA12 is not stimulated by CaM. Moreover, full length ACA12 is able to rescue a yeast mutant deficient in calcium pumps.

ACA12 is a deregulated isoform of plasma membrane Ca2+-ATPase of Arabidopsis thaliana / M. Limonta, S. Romanowsky, C. Olivari, M.C. Bonza, L. Luoni, A. Rosenberg, J.F. Harper, M.I. De Michelis. - In: PLANT MOLECULAR BIOLOGY. - ISSN 0167-4412. - 84:4-5(2014 Mar), pp. 387-397. [10.1007/s11103-013-0138-9]

ACA12 is a deregulated isoform of plasma membrane Ca2+-ATPase of Arabidopsis thaliana

M. Limonta;C. Olivari;M.C. Bonza;L. Luoni;M.I. De Michelis
2014-03

Abstract

Plant auto-inhibited Ca2+-ATPases (ACA) are crucial in defining the shape of calcium transients and therefore in eliciting plant responses to various stimuli. Arabidopsis thaliana genome encodes ten ACA isoforms that can be divided into four clusters based on gene structure and sequence homology. While isoforms from clusters 1, 2 and 4 have been characterized, virtually nothing is known about members of cluster 3 (ACA12 and ACA13). Here we show that a GFP-tagged ACA12 localizes at the plasma membrane and that expression of ACA12 rescues the phenotype of partial male sterility of a null mutant of the plasma membrane isoform ACA9, thus providing genetic evidence that ACA12 is a functional plasma membrane-resident Ca2+-ATPase. By ACA12 expression in yeast and purification by CaM-affinity chromatography, we show that, unlike other ACAs, the activity of ACA12 is not stimulated by CaM. Moreover, full length ACA12 is able to rescue a yeast mutant deficient in calcium pumps.
Arabidopsis thaliana; Ca2+-ATPase; Calmodulin; Plasma membrane
Settore BIO/04 - Fisiologia Vegetale
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/233312
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