Subcellular localization of rice acyl-CoA-binding proteins (ACBPs) indicates that OsACBP6::GFP is targeted to the peroxisomes
Article first published online: 16 APR 2014
© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust
Volume 203, Issue 2, pages 469–482, July 2014
How to Cite
Meng, W., Hsiao, A.-S., Gao, C., Jiang, L. and Chye, M.-L. (2014), Subcellular localization of rice acyl-CoA-binding proteins (ACBPs) indicates that OsACBP6::GFP is targeted to the peroxisomes. New Phytologist, 203: 469–482. doi: 10.1111/nph.12809
- Issue published online: 19 JUN 2014
- Article first published online: 16 APR 2014
- Manuscript Accepted: 12 MAR 2014
- Manuscript Received: 10 DEC 2013
- Wilson and Amelia Wong Endowment Fund
- University of Hong Kong
- acyl-CoA-binding protein (ACBP);
- Arabidopsis thaliana ;
- indole-3-butyric acid;
- jasmonic acid;
- Oryza sativa (rice);
- peroxisomal β-oxidation;
- subcellular localization
- Acyl-CoA-binding proteins (ACBPs) show conservation at the acyl-CoA-binding (ACB) domain which facilitates binding to acyl-CoA esters. In Arabidopsis thaliana, six ACBPs participate in development and stress responses. Rice (Oryza sativa) also contains six genes encoding ACBPs. We investigated differences in subcellular localization between monocot rice and eudicot A. thaliana ACBPs.
- The subcellular localization of the six OsACBPs was achieved via transient expression of green fluorescence protein (GFP) fusions in tobacco (Nicotiana tabacum) epidermal cells, and stable transformation of A. thaliana. As plant ACBPs had not been reported in the peroxisomes, OsACBP6::GFP localization was confirmed by transient expression in rice sheath cells. The function of OsACBP6 was investigated by overexpressing 35S::OsACBP6 in the peroxisomal abc transporter1 (pxa1) mutant defective in peroxisomal fatty acid β-oxidation.
- As predicted, OsACBP1::GFP and OsACBP2::GFP were localized to the cytosol, and OsACBP4::GFP and OsACBP5::GFP to the endoplasmic reticulum (ER). However, OsACBP3::GFP displayed subcellular multi-localization while OsACBP6::GFP was localized to the peroxisomes. 35S::OsACBP6-OE/pxa1 lines showed recovery in indole-3-butyric acid (IBA) peroxisomal β-oxidation, wound-induced VEGETATIVE STORAGE PROTEIN1 (VSP1) expression and jasmonic acid (JA) accumulation.
- These findings indicate a role for OsACBP6 in peroxisomal β-oxidation, and suggest that rice ACBPs are involved in lipid degradation in addition to lipid biosynthesis.