Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop. (Articolo in rivista)

Type
Label
  • Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop. (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.febslet.2004.08.003 (literal)
Alternative label
  • Luoni L.; Meneghelli S.; Bonza M.C.; DeMichelis M.I. (2004)
    Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop.
    in FEBS letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Luoni L.; Meneghelli S.; Bonza M.C.; DeMichelis M.I. (literal)
Pagina inizio
  • 20 (literal)
Pagina fine
  • 24 (literal)
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  • 574 (literal)
Rivista
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  • 5 (literal)
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  • 1-3 (literal)
Note
  • Google Scholar (literal)
  • ISI Web of Science (WOS) (literal)
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  • Dipartimento di Biologia \"L. Gorini\", Università di Milano, CNR Istituto di Biofisica - Sezione di Milano, via G. Celoria 26, 20133 Milano, Italy (literal)
Titolo
  • Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop. (literal)
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. (literal)
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