Accumulation of a lectin-like breakdown product of beta-conglutin catabolism in cotyledons of germinating Lupinus albus L. seeds

During germination of Lupinus albus seeds, a 20-kDa polypeptide accumulates in the cotyledons of 4-d-old plants (Ferreira et al., 1995b, J Exp Bot 46: 211—219). Immunological, polypeptide cleavage with cyanogen bromide and amino acid sequencing experiments indicate that the 20-kDa polypeptide and ub...

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Bibliographic Details
Published in:	Planta Vol. 203; no. 1; pp. 26 - 34
Main Authors:	Rodrigues dos Ramos, P.C, Seixas Boavida Ferreira, R.M. de, Franco, E, Nascimento Teixeira, A.R. (Universidade Nova de Lisboa (Portugal). Instituto de Tecnologia Quimica e Biologica)
Format:	Journal Article
Language:	English
Published:	Berlin Springer-Verlag 01-09-1997 Springer
Subjects:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Agronomy. Soil science and plant productions Amino Acid Sequence AMINOSAEURESEQUENZ Animals Antibodies Biological and medical sciences Biotechnology CALCIO CALCIUM CATABOLISM CATABOLISME CATABOLISMO Chromatography, Ion Exchange CONGLUTIN COTILEDONES COTYLEDON Cotyledon - physiology COTYLEDONS Economic plant physiology Electrophoresis, Polyacrylamide Gel Embryo development. Germination ENZYMIC ACTIVITY EXPRESION GENICA EXPRESSION DES GENES Fabaceae - physiology FISIOLOGIA VEGETAL Fundamental and applied biological sciences. Psychology Gels GENE EXPRESSION GERMINACION GERMINATION Germination and dormancy GLICOPROTEINAS Globulins GLYCOPROTEINE GLYCOPROTEINS GRAINE Growth and development Immunoblotting IMMUNOLOGICAL TECHNIQUES LECTIN Lectins Lectins - isolation & purification Lectins - metabolism LUPINUS ALBUS METABOLISM METABOLISME METABOLISMO Molecular Sequence Data Molecular Weight PEPTIDE Peptide Fragments - chemistry Peptide Fragments - isolation & purification PEPTIDES PEPTIDOS Phosphatases PHYSIOLOGIE VEGETALE Plant Lectins PLANT PHYSIOLOGY Plant physiology and development Plant Proteins - chemistry Plant Proteins - isolation & purification Plant Proteins - metabolism Plants, Medicinal POLYPEPTID PROTEINAS PROTEINE PROTEINS Rabbits Rats Seed Storage Proteins Seedling growth SEEDS Seeds - physiology SEMILLA Sequence Alignment Sequence Homology, Amino Acid SPEICHERPROTEIN STOFFWECHSEL TECHNIQUE IMMUNOLOGIQUE TECNICAS INMUNOLOGICAS UBIQUITIN Ubiquitins VICILIN Lectin Storage protein Purification Germination Homology Immunological method Characterization Leguminosae Polypeptide Protein synthesis Dicotyledones Seed Angiospermae Lupinus albus Spermatophyta Fodder crop Aminoacid sequence
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Summary:	During germination of Lupinus albus seeds, a 20-kDa polypeptide accumulates in the cotyledons of 4-d-old plants (Ferreira et al., 1995b, J Exp Bot 46: 211—219). Immunological, polypeptide cleavage with cyanogen bromide and amino acid sequencing experiments indicate that the 20-kDa polypeptide and ubiquitin are structurally unrelated. However there is a strong sequence homology between the 20-kDa polypeptide and the vicilin-like storage proteins from pea and soybean. Our results indicate that the 20-kDa polypeptide is an intermediate breakdown product of β-conglutin catabolism, the vicilin-like storage protein from L. albus, and that its interaction with anti-ubiquitin antibodies results from the recognition of the antibodies by the 20-kDa polypeptide rather than by the opposite. Besides rabbit anti-ubiquitin antibodies, the 20-kDa polypeptide interacts with a variety of glycoproteins, including immunoglobulin G from several animal species, peroxidase and alkaline phosphatase, suggesting that it possesses a lectin-type activity. Its activity is resistant to sodium dodecyl sulfate or methanol treatments, boiling and autoclaving. Purification of the 20-kDa polypeptide and immunological studies with anti-20-kDa-polypeptide antibodies showed that the non-glycosylated polypeptide is part of a glycoprotein with an estimated molecular mass of 210 kDa, composed of several types of structurally related subunit with molecular masses ranging from 14 to 50 kDa. Purified native protein containing the 20-kDa polypeptide self-aggregates in a calcium-dependent manner as reported for some glycosylated lectins. The possible physiological function of the 20-kDa polypeptide is discussed.
Bibliography:	F60 1997G93811 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0032-0935 1432-2048
DOI:	10.1007/s004250050161