Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop

FEBS Letters
Laura LuoniMaria Ida DeMichelis

Abstract

Type IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppressed by calmodulin (CaM) binding. Here, we show that a peptide (6His-1M-I116) corresponding to the first 116 aminoacids (aa) of At-ACA8, the first cloned isoform of Arabidopsis thaliana plasma membrane Ca2+-ATPase, inhibits the activity of the enzyme deprived of the N-terminus by controlled trypsin treatment 10-fold more efficiently than a peptide (41I-T63) corresponding only to the CaM-binding site. A peptide (268E-W348) corresponding to 81 aa of the small cytoplasmic loop of At-ACA8 binds peptide 6His-1M-I116 immobilized on Ni-NTA agarose. Peptide 268E-W348 stimulates Ca2+-ATPase activity. Its effect is not additive with that of CaM and is suppressed by tryptic cleavage of the N-terminus. These results provide the first functional identification of a site of intramolecular interaction with the terminal auto-inhibitory domain of type IIB Ca2+-ATPases.

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Citations

May 13, 2006·Journal of Bioenergetics and Biomembranes·Lone BaekgaardMichael G Palmgren
Aug 7, 2013·Journal of Experimental Botany·Kazi Md Kamrul HudaNarendra Tuteja
Nov 17, 2007·Journal of Biochemistry·Silvia MeneghelliMaria Ida De Michelis
Dec 17, 2008·The New Phytologist·Anna Amtmann, Michael R Blatt
Nov 16, 2010·FEBS Letters·Maria Cristina Bonza, Laura Luoni

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