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The Two Major Types of Plant Plasma Membrane
H+-ATPases Show Different Enzymatic Properties and Confer
Differential pH Sensitivity of Yeast Growth1
Hong Luo,
Pierre Morsomme, and
Marc Boutry*
Unité de Biochimie Physiologique, Université Catholique
de Louvain, Place Croix du Sud 2-20, B-1348 Louvain-la-Neuve,
Belgium
The proton-pumping ATPase
(H+-ATPase) of the plant plasma membrane is encoded by two
major gene subfamilies. To characterize individual
H+-ATPases, PMA2, an H+-ATPase isoform of
tobacco (Nicotiana plumbaginifolia), was expressed in
Saccharomyces cerevisiae and found to functionally
replace the yeast H+-ATPase if the external pH was kept
above 5.0 (A. de Kerchove d'Exaerde, P. Supply, J.P. Dufour, P. Bogaerts, D. Thinès, A. Goffeau, M. Boutry [1995] J Biol
Chem 270: 23828-23837). In the present study we replaced the
yeast H+-ATPase with PMA4, an H+-ATPase isoform
from the second subfamily. Yeast expressing PMA4 grew at a pH as low as
4.0. This was correlated with a higher acidification of the external
medium and an approximately 50% increase of ATPase activity compared
with PMA2. Although both PMA2 and PMA4 had a similar pH optimum
(6.6-6.8), the profile was different on the alkaline side. At pH 7.2 PMA2 kept more than 80% of the maximal activity, whereas that of PMA4
decreased to less than 40%. Both enzymes were stimulated up to 3-fold
by 100 µg/mL lysophosphatidylcholine, but this stimulation vanished
at a higher concentration in PMA4. These data demonstrate functional differences between two plant H+-ATPases expressed in the
same heterologous host. Characterization of two PMA4 mutants selected
to allow yeast growth at pH 3.0 revealed that mutations within the
carboxy-terminal region of PMA4 could still improve the enzyme,
resulting in better growth of yeast cells.
1
This work was supported by the Interuniversity
Poles of Attraction Program (Belgian State Prime Minister's Office,
Federal Office for Scientific, Technical and Cultural Affairs), by the European Community's BIOTECH Program, and by the Belgian Fund for
Scientific Research.
*
Corresponding author; e-mail boutry{at}fysa.ucl.ac.be; fax
32-10-47-38-72.
Plant Physiol. (1999) 119: 627-634
Copyright Clearance Center: 0032-0889/99/119//08
© 1999 American Society of Plant Physiologists
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