Domain construction of cherry-tomato lectin: Relation to newly found 42-kDa protein

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2001-01, Vol.65 (1), p.86-93
• Main Authors: Naito, Y. (Chiba Univ., Matsudo (Japan). Faculty of Horticulture), Minamihara, T, Ando, A, Marutani, T, Oguri, S, Nagata, Y
• Format: Article
• Language: English
• Subjects: Agronomy. Soil science and plant productions; Amino Acid Motifs; Amino Acid Sequence; AMINO ACIDS; Amino Acids - chemistry; Biological and medical sciences; CHEMICAL STRUCTURE; CHERRY TOMATOES; CHITIN; Chitin - metabolism; Cys-rich chitin-binding domain; Economic plant physiology; Fructification, ripening. Postharvest physiology; FRUIT; Fruit - chemistry; Fundamental and applied biological sciences. Psychology; Growth and development; Hyp-rich glycoprotein domain; Immunoblotting; Lectin-related 42-kDa protein; LECTINS; Lectins - chemistry; Lectins - genetics; Lectins - isolation & purification; Lectins - metabolism; Lycopersicon esculentum - chemistry; Lycopersicon esculentum - genetics; Lycopersicon esculentum - physiology; Lycopersicon esculentum var. cherry; Molecular Sequence Data; Plant Lectins; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - metabolism; Protein Structure, Tertiary; PROTEINS; RIPENING; Structure of cherry-tomato lectin
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.65.86

In the early stage of ripening of cherry-tomato fruits (Lycopersicon esculentum var. cherry), the lectin activity increased logarithmically and reached a plateau at day 10 after flowering. During purification of lectin from ripe and unripe fruits, a 42-kDa protein was found abundantly in unripe fruits. The protein cross-reacted with anti-cherry-tomato-lectin serum, retained chitinbinding ability, but showed no lectin activity. Comparative studies between the structure of the lectin and the 42-kDa protein were done. N-Terminal amino acid sequences of the lectin, peptides derived from the S-pyridylethylated lectin, and fragments generated by limited proteolysis of the native lectin showed that the lectin was comprised of three domains, Hyp-rich, Cysrich, and Gln-rich, and the alignment of them was as this order from the N-terminus. Studies on the 42-kDa protein showed that it contained two of the three domains, Cys-rich and Gln-rich, but the amino acid sequence analysis showed that the protein should be a product of another gene.