title: The regulatory domain of fungal and plant plasma membrane H(+)-ATPase.
abstract: The activity of fungal and plant plasma membrane H(+)-ATPases seems to be regulated by modulation of the interaction of an inhibitory domain at the C-terminus with the active site. In the yeast ATPase, a mutation at the active site (Ala547- > Val) and a deletion of the C-terminus result in constitutive activation. A double Ser911- > Ala, Thr912- > Ala mutation at the C-terminus (defining putative phosphorylation sites) locks the enzyme in the inhibited state and can be suppressed by the Ala547- > Val mutation at the active site. This provides genetic evidence for domain interaction. In plant ATPase, proteolytic removal of the C-terminus also results in constitutive activation. A peptide covering a region of the plant C-terminus with homology to the yeast C-terminus inhibits the truncated plant ATPase. This suggests similar regulatory mechanisms in fungal and plant ATPases.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Serrano
authors.forename: F
authors.initials: F
authors.lastname: Portillo
authors.forename: B C
authors.initials: BC
authors.lastname: Monk
authors.forename: M G
authors.initials: MG
authors.lastname: Palmgren
mesh_terms: D002462:Cell Membrane / Q000201:enzymology*; D005658:Fungi / Q000201:enzymology*; D010944:Plants / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000378:metabolism*
chemical_list: D006180:Proton-Translocating ATPases