Characterization of a cDNA clone encoding a Brassica napus 12 S protein (cruciferin) subunit. Relationship between precursors and mature chains

Cruciferin (12 S globulin) is a large, neutral, oligometric protein synthesized in rapeseed (Brassica napus) during seed development. It is the major seed protein and is composed of six subunit pairs. Each of these pairs is synthesized as a precursor containing one heavy alpha-chain and one light be...

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Bibliographic Details
Published in:The Journal of biological chemistry 1990-02, Vol.265 (5), p.2720-2723
Main Authors: RODIN, J, ERICSON, M. L, JOSEFSSON, L.-G, RASK, L
Format: Article
Language:English
Subjects:
Allergens
Amino Acid Sequence
Antigens, Plant
Base Sequence
Biological and medical sciences
Brassica - genetics
Cloning, Molecular
Codon - genetics
cruciferin
DNA - genetics
Fundamental and applied biological sciences. Psychology
Gene Library
genes
Genes. Genome
Macromolecular Substances
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Plant Proteins - genetics
Plant Proteins - isolation & purification
Protein Precursors - genetics
Repetitive Sequences, Nucleic Acid
Restriction Mapping
Seed Storage Proteins
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Summary:Cruciferin (12 S globulin) is a large, neutral, oligometric protein synthesized in rapeseed (Brassica napus) during seed development. It is the major seed protein and is composed of six subunit pairs. Each of these pairs is synthesized as a precursor containing one heavy alpha-chain and one light beta-chain. Electrophoretic analysis of cruciferin showed that four different alpha- and four different beta-chains exist. A cruciferin clone was selected from an embryo cDNA library. This clone, pCRU1, contains a 1518-base pair open reading frame corresponding to a truncated NH2-terminal signal sequence followed by an alpha-chain of 296 and a beta-chain of 190 amino acid residues. Individual cruciferin chains as well as peptides thereof were subjected to NH2-terminal amino acid sequence analysis. The sequences obtained from a specific alpha- and beta-chain pair (alpha 1 and beta 1) showed total identity with the deduced amino acid sequence from pCRU1. Further comparisons revealed that a previously characterized cruciferin cDNA clone encodes one of the precursors for the closely related alpha 2/ alpha 3-beta 2/beta 3 subunits. The deduced amino acid sequences of the two cDNA clones display 64% similarity.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)39861-8