A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-atpase (AHA1 isoform): site and mechanism of action on H+-atpase activity differ from those of 14-3-3 proteins (Articolo in rivista)

Type
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  • A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-atpase (AHA1 isoform): site and mechanism of action on H+-atpase activity differ from those of 14-3-3 proteins (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Morandini P. 1, Valera M. 2, Albumi C. 1, Bonza M.C. 1, Giacometti S. 2, Ravera G. 2, Murgia I. 1, Soave C. 1, De Michelis M.I. 1 (2002)
    A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-atpase (AHA1 isoform): site and mechanism of action on H+-atpase activity differ from those of 14-3-3 proteins
    in Plant journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Morandini P. 1, Valera M. 2, Albumi C. 1, Bonza M.C. 1, Giacometti S. 2, Ravera G. 2, Murgia I. 1, Soave C. 1, De Michelis M.I. 1 (literal)
Pagina inizio
  • 487 (literal)
Pagina fine
  • 497 (literal)
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  • 31 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • La pubblicazione descrive l'identificazione e una prima caratterizzazione di un nuovo interattore della pompa protonica della membrana plasmatica di Arabidopsis thaliana. La nuova proteina รจ stata identificata con il metodo del doppio ibrido e appartiene ad una famiglia multigenica con numerosi membri sia in Arabidopsis che nelle altre specie vegetali. E' interessante il fatto che il meccanismo di azione sulla pompa sembra essere diverso da quelli fino ad ora caratterizzati. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1: CNR; 2: Uni Milano (literal)
Titolo
  • A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-atpase (AHA1 isoform): site and mechanism of action on H+-atpase activity differ from those of 14-3-3 proteins (literal)
Abstract
  • Using the two-hybrid technique we identified a novel protein whose N- terminal 88 amino acids (aa) interact with the C-terminal regulatory domain of the plasma membrane (PM) H+-ATPase from Arabidopsis thaliana (aa 847-949 of isoform AHA1). The corresponding gene has been named Ppi1 for Protonpumpinteractor 1. The encoded protein is 612 aa long and rich in charged and polar residues, except for the extreme C-terminus, where it presents a hydrophobic stretch of 24 aa. Several genes in the A. thaliana genome and many ESTs from different plant species share significant similarity (50-70% at the aa level over stretches of 200-600 aa) to Ppi1. The PPI1 N-terminus, expressed in bacteria as a fusion protein with either GST or a His-tag, binds the PM H+-ATPase in overlay experiments. The same fusion proteins and the entire coding region fused to GST stimulate H+- ATPase activity. The effect of the His-tagged peptide is synergistic with that of fusicoccin (FC) and of tryptic removal of a C-terminal 10 kDa fragment. The His-tagged peptide binds also the trypsinised H+-ATPase. Altogether these results indicate that PPI1 N-terminus is able to modulate the PM H+-ATPase activity by binding to a site different from the 14-3-3 binding site and is located upstream of the trypsin cleavage site. (literal)
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