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Plant Cell, Vol. 12, 2441-2454, December 2000, Copyright © 2000, American Society of Plant Physiologists

Chilling Tolerance in Arabidopsis Involves ALA1, a Member of a New Family of Putative Aminophospholipid Translocases

Eric Gomèsa, Mia Kyed Jakobsena, Kristian B. Axelsena, Markus Geislera, and Michael Gjedde Palmgrena
a Department of Plant Biology, The Royal Veterinary and Agricultural University, DK-1871 Frederiksberg C, Denmark

Correspondence to: Eric Gomès, egomes{at}upmail.univ-poitiers.fr (E-mail), 33-549-45-41-86 (fax)

The lipid composition of membranes is a key determinant for cold tolerance, and enzymes that modify membrane structure seem to be important for low-temperature acclimation. We have characterized ALA1 (for aminophospholipid ATPase1), a novel P-type ATPase in Arabidopsis that belongs to the gene family ALA1 to ALA11. The deduced amino acid sequence of ALA1 is homologous with those of yeast DRS2 and bovine ATPase II, both of which are putative aminophospholipid translocases. ALA1 complements the deficiency in phosphatidylserine internalization into intact cells that is exhibited by the drs2 yeast mutant, and expression of ALA1 results in increased translocation of aminophospholipids in reconstituted yeast membrane vesicles. These lines of evidence suggest that ALA1 is involved in generating membrane lipid asymmetry and probably encodes an aminophospholipid translocase. ALA1 complements the cold sensitivity of the drs2 yeast mutant. Downregulation of ALA1 in Arabidopsis results in cold-affected plants that are much smaller than those of the wild type. These data suggest a link between regulation of transmembrane bilayer lipid asymmetry and the adaptation of plants to cold.




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