Plant and Cell Physiology Advance Access originally published online on July 16, 2008
Plant and Cell Physiology 2008 49(9):1390-1395; doi:10.1093/pcp/pcn103
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Short Communication |
A Unique Caleosin in Oil Bodies of Lily Pollen
1 Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung 402, Taiwan
2 Institute of Plant and Microbial Biology, Academia Sinica, Taipei 115, Taiwan
3 Agricultural Biotechnology Research Center, Academia Sinica, Taipei 115, Taiwan
*Corresponding author: E-mail, TCTZEN{at}dragon.nchu.edu.tw: Fax, +886-4-22853527.
| Abstract |
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In view of the recent isolation of stable oil bodies as well as a unique oleosin from lily pollen, this study examined whether other minor proteins were present in this lipid-storage organelle. Immunological cross-recognition using antibodies against three minor oil-body proteins from sesame suggested that a putative caleosin was specifically detected in the oil-body fraction of pollen extract. A cDNA fragment encoding this putative pollen caleosin, obtained by PCR cloning, was confirmed by immunodetection and MALDI-MS analyses of the recombinant protein over-expressed in Escherichia coli and the native form. Caleosin in lily pollen oil bodies seemed to be a unique isoform distinct from that in lily seed oil bodies.
Keywords: Caleosin - Lily (Lilium longiflorum Thunb.) - Oil bodies - Oleosin - Pollen
Abbreviations: PL(s), phospholipid(s); TAG(s), triacylglycerol(s).
(Received May 15, 2008; Accepted July 13, 2008)
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