A unique caleosin in oil bodies of lily pollen

Plant Cell Physiol. 2008 Sep;49(9):1390-5. doi: 10.1093/pcp/pcn103. Epub 2008 Jul 16.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / genetics*
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Genes, Plant
  • Lilium / chemistry
  • Lilium / genetics*
  • Molecular Sequence Data
  • Phylogeny
  • Plant Oils / chemistry
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Pollen / chemistry
  • Pollen / genetics*
  • RNA, Plant / genetics
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Calcium-Binding Proteins
  • Plant Oils
  • Plant Proteins
  • RNA, Plant
  • caleosin protein, Sesamum indicum

Associated data

  • GENBANK/EF015588