| Abstract: | In plant seeds, the storage triacylglycerol is packed in discrete particles called lipid bodies which consist of a lipid core surrounded by a phospholipid monolayer with embedded proteins. We have cloned and sequenced a nearly full-length cDNA for the major protein (L3) associated with the lipid bodies of maize. The L3-cDNA clone was identified by hybrid-selected translation analysis and contains the complete 3' noncoding region and an open reading frame of 432 nucleotides. This open reading frame encodes a polypeptide with amino acid composition, hydrophobicity, and predicted protease digestion pattern which correlate well with those of the authentic L3 protein. Analyses of predicted secondary structure and local hydropathy of the deduced amino acid sequence suggest three structural domains in the protein. An internal domain of 72 contiguous hydrophobic or neutral amino acids is bounded at the amino-terminal side by a hydrophilic alpha-helix and on the carboxyl-terminal side by an amphipathic alpha-helix. The data suggest that L3 is uniquely suited to interact with both lipid and phospholipid moieties of the lipid body. A simple model for the topology of L3 on the lipid body is proposed. The unusual structure of the lipid body protein is discussed and compared to those of the two well-studied classes of lipid-associated proteins, apolipoproteins and intrinsic membrane proteins. |
