The regulatory domain of fungal and plant plasma membrane H+-ATPase
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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.
Original language | English |
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Journal | Acta Physiologica Scandinavica, Supplement |
Volume | 146 |
Issue number | 607 |
Pages (from-to) | 131-136 |
Number of pages | 6 |
ISSN | 0302-2994 |
Publication status | Published - 1992 |
ID: 245002215