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JXB Advance Access originally published online on March 13, 2009
Journal of Experimental Botany 2009 60(6):1839-1848; doi:10.1093/jxb/erp057
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Characterization of two cotton cDNAs encoding trans-2-enoyl-CoA reductase reveals a putative novel NADPH-binding motif

Wen-Qiang Song1,2, Yong-Mei Qin1,2,*, Mihoko Saito3, Tsuyoshi Shirai3, François M. Pujol4, Alexander J. Kastaniotis4, J. Kalervo Hiltunen4 and Yu-Xian Zhu1,2

1National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, 100871, China
2Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing, 100871, China
3Department of Bioscience, Nagahama Institute of Bioscience and Technology, 1266 Tamura, Nagahama 526-0829, Japan
4Biocenter Oulu and Department of Biochemistry, University of Oulu, PO Box 3000, FI-90014 Oulu, Finland

* To whom correspondence should be addressed. E-mail: qinym{at}pku.edu.cn

Very long chain fatty acids are important components of plant lipids, suberins, and cuticular waxes. Trans-2-enoyl-CoA reductase (ECR) catalyses the fourth reaction of fatty acid elongation, which is NADPH dependent. In the present study, the expression of two cotton ECR (GhECR) genes revealed by quantitative RT-PCR analysis was up-regulated during cotton fibre elongation. GhECR1 and 2 each contain open reading frames of 933 bp in length, both encoding proteins consisting of 310 amino acid residues. GhECRs show 32% identity to Saccharomyces cerevisiae Tsc13p at the deduced amino acid level, and the GhECR genes were able to restore the viability of the S. cerevisiae haploid tsc13-deletion strain. A putative non-classical NADPH-binding site in GhECR was predicted by an empirical approach. Site-directed mutagenesis in combination with gas chromatography–mass spectrometry analysis suggests that G(5X)IPXG presents a putative novel NADPH-binding motif of the plant ECR family. The data suggest that both GhECR genes encode functional enzymes harbouring non-classical NADPH-binding sites at their C-termini, and are involved in fatty acid elongation during cotton fibre development.

Key words: 2-Enoyl-CoA reductase, fatty acid elongation, Gossypium hirsutum, NADPH-binding motif, very long chain fatty acid

Received 10 November 2008; Revised 5 February 2009 Accepted 13 February 2009


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