cDNA cloning, primary structure, and in vitro biosynthesis of the DB58 lectin from Dolichos biflorus

Previous studies have shown that the Dolichos biflorus plant contains a lectin in its stems and leaves, called DB58, that is closely related to the D. biflorus seed lectin. DB58 is a heterodimer composed of two closely related subunits. Immunoprecipitation of total translation products from D. biflo...

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-10, Vol.263 (29), p.14648-14653
Main Authors: Schnell, D J, Etzler, M E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Biological and medical sciences
biosintesis
biosynthese
biosynthesis
Biotechnology
Blotting, Northern
carbohidratos
carbohydrates
clonacion
clonage
cloning
Cloning, Molecular
DNA - genetics
DNA - isolation & purification
DNA Restriction Enzymes
Fundamental and applied biological sciences. Psychology
gene
Genes
Genetic engineering
Genetic technics
glucide
lablab purpureus
lectina
lectine
lectins
Lectins - biosynthesis
Lectins - genetics
Methods. Procedures. Technologies
Molecular Sequence Data
Nucleic Acid Hybridization
Nucleotide Mapping
Plant Lectins
Plants - genetics
Plants - metabolism
Protein Biosynthesis
proteinas
proteine
proteins
RNA, Messenger
Transcription, Genetic
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Summary:Previous studies have shown that the Dolichos biflorus plant contains a lectin in its stems and leaves, called DB58, that is closely related to the D. biflorus seed lectin. DB58 is a heterodimer composed of two closely related subunits. Immunoprecipitation of total translation products from D. biflorus stem and leaf mRNA suggests a single polypeptide precursor for both of these subunits. Several identical cDNA clones representing the entire coding region of the DB58 mRNA have been isolated from a D. biflorus stem and leaf cDNA library. The DB58 cDNA represents an mRNA encoding a polypeptide of Mr = 29,545. The predicted polypeptide is equal in length to the larger subunit of DB58 with the addition of a 22-amino acid amino-terminal signal sequence. The sequence of the DB58 lectin exhibits 84% homology to the D. biflorus seed lectin at the amino acid level, suggesting that these lectins are encoded by differentially expressed genes and may have evolved to carry out tissue-specific functions. Comparison of the DB58 sequence to other leguminous seed lectins indicates a high degree of structural conservation.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)68086-X