Type IIB Ca2+-ATPases have a terminal autoinhibitory, domain the action of which is suppressed by calmodulin (CaM) binding. Here, we show that a peptide (6His-M-1-I-116) 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 (I-41-T-63) corresponding only to the CaM-binding site. A peptide (E-268-W-348) corresponding to 81 aa of the small cytoplasmic loop of At-ACA8 binds peptide (268)His-M-1-I-116 immobilized on Ni-NTA agarose. Peptide E-268-W-348 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 autoinhibitory domain of type IIB Ca2+-ATPases.

Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop / L. Luoni, S. Meneghelli, M.C. Bonza, M.I. De Michelis. - In: FEBS LETTERS. - ISSN 0014-5793. - 574:1-3(2004), pp. 20-24.

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

L. Luoni
Primo
;
S. Meneghelli
Secondo
;
M.C. Bonza
Penultimo
;
M.I. De Michelis
Ultimo
2004

Abstract

Type IIB Ca2+-ATPases have a terminal autoinhibitory, domain the action of which is suppressed by calmodulin (CaM) binding. Here, we show that a peptide (6His-M-1-I-116) 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 (I-41-T-63) corresponding only to the CaM-binding site. A peptide (E-268-W-348) corresponding to 81 aa of the small cytoplasmic loop of At-ACA8 binds peptide (268)His-M-1-I-116 immobilized on Ni-NTA agarose. Peptide E-268-W-348 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 autoinhibitory domain of type IIB Ca2+-ATPases.
aa, aminoacids; Arabidopsis thaliana; Auto-inhibition; Ca2+-ATPase; Calmodulin; CaM, calmodulin; Intramolecular interaction; Plasma membrane; PM, plasma membrane; TM, transmembrane domain
Settore BIO/04 - Fisiologia Vegetale
2004
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/27691
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