Stable oil bodies sheltered by a unique caleosin in cycad megagametophytes

Stable oil bodies of smaller sizes and higher thermostability were isolated from mature cycad ( Cycas revoluta) megagametophytes compared with those isolated from sesame seeds. Immunological cross-recognition revealed that cycad oil bodies contained a major protein of 27 kDa, tentatively identified...

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Bibliographic Details
Published in:Plant physiology and biochemistry 2009-11, Vol.47 (11), p.1009-1016
Main Authors: Jiang, Pei-Luen, Chen, Jeff C.F., Chiu, Shau-Ting, Tzen, Jason T.C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Calcium-Binding Proteins - genetics
Calcium-Binding Proteins - metabolism
Caleosin
Cloning, Molecular
Conserved Sequence
Cycad ( Cycas revoluta)
Cycadophyta
Cycadopsida - genetics
Cycadopsida - metabolism
Cycas revoluta
DNA, Complementary - isolation & purification
Escherichia coli
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
Mass Spectrometry
Megagametophyte
Molecular Sequence Data
Oil bodies
Oleosin
Organelles - metabolism
Phospholipids
Plant Oils - chemistry
Plant Oils - isolation & purification
Plant Oils - metabolism
Plant physiology and development
Plant Proteins - genetics
Plant Proteins - metabolism
Polymerase Chain Reaction
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RNA, Plant - isolation & purification
Sesamum
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Triglycerides
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Description
Summary:Stable oil bodies of smaller sizes and higher thermostability were isolated from mature cycad ( Cycas revoluta) megagametophytes compared with those isolated from sesame seeds. Immunological cross-recognition revealed that cycad oil bodies contained a major protein of 27 kDa, tentatively identified as caleosin, while oleosin, the well-known structural protein, was apparently absent. Mass spectrometric analysis showed that the putative cycad caleosin possessed a tryptic fragment of 15 residues matching to that of a theoretical moss caleosin. A complete cDNA fragment encoding this putative caleosin was obtained by PCR cloning using a primer designed according to the tryptic peptide and another one designed according to a highly conservative region among diverse caleosins. The identification of this clone was subsequently confirmed by immunodetection and MALDI-MS analyses of its recombinant fusion protein over-expressed in Escherichia coli and the native form from cycad oil bodies. Stable artificial oil bodies were successfully constituted with triacylglycerol, phospholipid and the recombinant fusion protein containing the cycad caleosin. These results suggest that stable oil bodies in cycad megagametophytes are mainly sheltered by a unique structural protein caleosin.
ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2009.07.004