The Arabidopsis det3 mutant reveals a central role for the vacuolar H(+)-ATPase in plant growth and development

• Published in: Genes & development Vol. 13; no. 24; pp. 3259 - 3270
• Main Authors: Schumacher, K, Vafeados, D, McCarthy, M, Sze, H, Wilkins, T, Chory, J
• Format: Journal Article
• Language: English
• Published: United States Cold Spring Harbor Laboratory Press 15.12.1999
• Subjects: Amino Acid Sequence; Animals; Arabidopsis - enzymology; Arabidopsis - genetics; Arabidopsis - growth & development; Cloning, Molecular; Evolution, Molecular; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Humans; Light; Molecular Sequence Data; Phylogeny; Proton Pumps - metabolism; Proton-Translocating ATPases - chemistry; Proton-Translocating ATPases - genetics; Proton-Translocating ATPases - metabolism; Research Paper; Sequence Alignment; Sequence Homology, Amino Acid; Vacuolar Proton-Translocating ATPases
• DOI: 10.1101/gad.13.24.3259
• ISSN: 0890-9369

In all multicellular organisms growth and morphogenesis must be coordinated, but for higher plants, this is of particular importance because the timing of organogenesis is not fixed but occurs in response to environmental constraints. One particularly dramatic developmental juncture is the response of dicotyledonous seedlings to light. The det3 mutant of Arabidopsis develops morphologically as a light-grown plant even when it is grown in the dark. In addition, it shows organ-specific defects in cell elongation and has a reduced response to brassinosteroids (BRs). We have isolated the DET3 gene by positional cloning and provide functional and biochemical evidence that it encodes subunit C of the vacuolar H(+)-ATPase (V-ATPase). We show that the hypocotyl elongation defect in the det3 mutant is conditional and provide evidence that this is due to an alternative mechanism of V-ATPase assembly. Together with the expression pattern of the DET3 gene revealed by GFP fluorescence, our data provide in vivo evidence for a role for the V-ATPase in the control of cell elongation and in the regulation of meristem activity.