期刊
PLANT MOLECULAR BIOLOGY
卷 68, 期 6, 页码 571-583出版社
SPRINGER
DOI: 10.1007/s11103-008-9392-7
关键词
Acyl-CoA-binding protein; Autofluorescence-tagged protein; Cytosol; Galactolipids; Lipid metabolism; Phospholipids
资金
- Council of the Hong Kong Special Administrative Region, China [HKU7504/05 M]
- University of Hong Kong [10208034]
- Croucher Foundation
- National Science Foundation [EPS 0236913, MCB 0455318, DBI 0521587]
- Kansas Technology Enterprise Corporation
- Kansas IDeA Network of Biomedical Research Excellence (INBRE) of National Institute of Health [P20RR16475]
- Kansas State University
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016475] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P20GM103418] Funding Source: NIH RePORTER
In Arabidopsis thaliana, acyl-CoA-binding proteins (ACBPs) are encoded by six genes, and they display varying affinities for acyl-CoA esters. Recombinant ACBP4 and ACBP5 have been shown to bind oleoyl-CoA esters in vitro. In this study, the subcellular localizations of ACBP4 and ACBP5 were determined by biochemical fractionation followed by western blot analyses using anti-ACBP4 and anti-ACBP5 antibodies and immuno-electron microscopy. Confocal microscopy of autofluorescence-tagged ACBP4 and ACBP5, expressed transiently in onion epidermal cells and in transgenic Arabidopsis, confirmed their expression in the cytosol. Taken together, ACBP4 and ACBP5 are available in the cytosol to bind and transfer cytosolic oleoyl-CoA esters. Lipid profile analysis further revealed that an acbp4 knockout mutant showed decreases in membrane lipids (digalactosyldiacylglycerol, monogalactosyldiacylglycerol, phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol) while acbp4-complemented lines attained levels similar to wild type, suggesting that ACBP4 plays a role in the biosynthesis of membrane lipids including galactolipids and phospholipids.
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