Style-specific and developmentally regulated accumulation of a glycosylated thaumatin/PR5-like protein in Japanese pear (Pyrus serotina Rahd.)

• Published in: Planta 1998-08, Vol.205 (4), p.514-521
• Main Authors: Sassa, H, Hirano, H
• Format: Article
• Language: English
• Subjects: Agronomy. Soil science and plant productions; Amino Acid Sequence; amino acid sequences; Amino acids; Base Sequence; Biological and medical sciences; chemical constituents of plants; Cloning, Molecular; Complementary DNA; concanavalin A; DNA, Complementary; DNA, Plant; Economic plant physiology; Flowering, floral biology, reproduction patterns; Fruit - genetics; Fruit - metabolism; Fundamental and applied biological sciences. Psychology; Gels; genbank/ab006009; Glycoproteins; Glycoproteins - chemistry; Glycoproteins - genetics; Glycosylation; Growth and development; histochemistry; isoelectric point; Molecular Sequence Data; molecular weight; nucleotide sequences; pathogenesis-related proteins; Plant cells; plant development; Plant physiology and development; Plant Proteins - chemistry; Plant Proteins - genetics; Plants; Pollen; Polymerase chain reaction; protein synthesis; Proteins; Pyrus pyrifolia; Sequence Analysis; Sequence Homology, Amino Acid; Sexual reproduction; Styles; Sweetening Agents; Vegetative and sexual reproduction, floral biology, fructification
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/s004250050350

The stylar proteins of Japanese pear (Pyrus serotina Rehd.) were analyzed by two-dimensional gel electrophoresis, and a 32-kDa protein with an isoelectric point of 4.8 was found to be a major component in the style. The 32-kDa protein was a soluble glycoprotein which reacted with concanavalin A. The 32-kDa protein specifically accumulated in the style in a developmentally regulated manner, but was not detected in the other floral organs and leaves. An oligonucleotide representing the N-terminal amino acid sequence of the 32-kDa protein was used to amplify a cDNA fragment by polymerase chain reaction (PCR). The generated PCR product was used to screen a style cDNA library. The selected cDNA clone encoded 244 amino acid residues containing the N-terminal sequence of the 32-kDa protein. The N-terminus of the protein was preceded by putative signal peptide of 22 amino acid residues. The 32-kDa protein showed significant homology with the thaumatin/PR5-like proteins, and was named PsTL1 (Pyrus serotina thaumatin-like protein 1). The possible biological role of PsTL1 in the styles is discussed.