A unique caleosin in oil bodies of lily pollen.
Plant Cell Physiol. 2008 Sep; 49(9):1390-5.PC

Abstract

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.

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Authors+Show Affiliations

Jiang PL
Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung 402, Taiwan.
Jauh GY
No affiliation info available
Wang CS
No affiliation info available
Tzen JT
No affiliation info available

MeSH

Amino Acid SequenceCalcium-Binding ProteinsCloning, MolecularElectrophoresis, Polyacrylamide GelGenes, PlantLiliumMolecular Sequence DataPhylogenyPlant OilsPlant ProteinsPollenRNA, PlantSequence AlignmentSequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18632804