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Stable Oil Bodies Sheltered by a Unique Oleosin in Lily Pollen

Jiang, Pei-Luen, Wang, Co-Shing, Hsu, Chia-Mei, Jauh, Guang-Yuh, Tzen, Jason T.C.
Plant & cell physiology 2007 v.48 no.6 pp. 812-821
DNA primers, Lilium longiflorum, body protein, complementary DNA, electron microscopy, lipid bodies, mass spectrometry, nucleotide sequences, oleosin, pollen, pollen germination, polymerase chain reaction, rice, seed oils, sequence analysis, surface proteins, vacuoles
Stable oil bodies were purified from mature lily (Lilium longiflorum Thunb.) pollen. The integrity of pollen oil bodies was maintained via electronegative repulsion and steric hindrance possibly provided by their surface proteins. Immunodetection revealed that a major protein of 18 kDa was exclusively present in pollen oil bodies and massively accumulated in late stages of pollen maturation. According to mass spectrometric analyses, this oil body protein possessed a tryptic fragment of 13 residues matching that of a theoretical rice oleosin. A complete cDNA fragment encoding this putative oleosin was obtained by PCR cloning with primers derived from its known 13-residue sequence. Sequence analysis as well as immunological non-cross-reactivity suggests that this pollen oleosin represents a distinct class in comparison with oleosins found in seed oil bodies and tapetum. In pollen cells observed by electron microscopy, oil bodies were presumably surrounded by tubular membrane structures, and encapsulated in the vacuoles after germination. It seems that pollen oil bodies are mobilized via a different route from that of glyoxysomal mobilization of seed oil bodies after germination.