Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana. (Articolo in rivista)

Type
Label
  • Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/jb/mvm218 (literal)
Alternative label
  • Meneghelli S.; Luoni L.; De Michelis M.I. (2008)
    Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana.
    in Journal of Biochemistry (Tokyo)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Meneghelli S.; Luoni L.; De Michelis M.I. (literal)
Pagina inizio
  • 253 (literal)
Pagina fine
  • 259 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 143 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopus (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biologia \"L. Gorini\", Università di Milano, CNR Istituto di Biofisica - Sezione di Milano (literal)
Titolo
  • Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana. (literal)
Abstract
  • We have studied the effect of heparin, a glycosaminoglycan widely used in releasing tags from fusion proteins, on isoform 8 of Arabidopsis thaliana PM Ca(2+)-ATPase (ACA8) expressed in Saccharomyces cerevisiae strain K616. Heparin stimulates hydrolytic activity of ACA8 with an estimated K(0.5) value for the complex of 15 +/- 1 microg ml(-1), which is unaffected by free [Ca(2+)]. Heparin increases V(max) up to 3-fold while it does not significantly affect the apparent K(m) for free Ca(2+) and for the nucleoside triphosphate substrate. The heparin effect is not additive with that of exogenous calmodulin and heparin is ineffective on a mutant devoid of the N-terminal auto-inhibitory domain (Delta74-ACA8). Altogether, these results indicate that heparin activation is due to partial suppression of the auto-inhibitory function of ACA8 N-terminus. Pull-down assays using heparin-agarose gel show that heparin directly interacts with ACA8. Binding to the heparin-agarose gel occurs also with a peptide reproducing ACA8 sequence (1)M-I(116). Several single-point mutations within ACA8 sequence A56-T63 significantly alter the enzyme response to heparin, suggesting that heparin interaction with this site may be involved in ACA8 activation. These results highlight a new difference between the plant PM Ca(2+)-ATPase and its animal counterpart, which is inhibited by heparin. (literal)
Prodotto di
Autore CNR

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it