Cloning and analysis of cDNAs encoding plant storage protein precursors View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-01

AUTHORS

Ronald R. D. Croy, Grantley W. Lycett, John A. Gatehouse, Jennifer N. Yarwood, Donald Boulter

ABSTRACT

The major storage protein in many legume seeds is legumin, a hexameric molecule of molecular weight (Mr) 360,000–400,000 consisting of six subunit pairs, each of which comprises a 40,000-Mr, acidic polypeptide linked by disulphide bonds to a 20,000-Mr, basic polypeptide1. We have recently shown that these subunit pairs are synthesized, in vivo and in vitro in Pisumand Vicia2,3, as a 60,000-Mr precursor polypeptide, putatively containing one copy each of the acidic and basic summits covalently linked together. We describe here the cloning and identification of cDNA sequences coding for the legumin precursor. Additionally, we have used these cDNAs to verify that the legumin mRNAs are of sufficient size to code for the precursor and to demonstrate the presence of four single-copy legumin genes in genomic DNA. Possible mechanisms for the processing of the legumin precursor are discussed. Identification of cloned cDNA sequences coding for vicilin, the secondary storage protein of Pisum sativum4, is also reported. More... »

PAGES

76

Journal

TITLE

Nature

ISSUE

5844

VOLUME

295

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/295076a0

DOI

http://dx.doi.org/10.1038/295076a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007285060


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53 schema:description The major storage protein in many legume seeds is legumin, a hexameric molecule of molecular weight (Mr) 360,000–400,000 consisting of six subunit pairs, each of which comprises a 40,000-Mr, acidic polypeptide linked by disulphide bonds to a 20,000-Mr, basic polypeptide1. We have recently shown that these subunit pairs are synthesized, in vivo and in vitro in Pisumand Vicia2,3, as a 60,000-Mr precursor polypeptide, putatively containing one copy each of the acidic and basic summits covalently linked together. We describe here the cloning and identification of cDNA sequences coding for the legumin precursor. Additionally, we have used these cDNAs to verify that the legumin mRNAs are of sufficient size to code for the precursor and to demonstrate the presence of four single-copy legumin genes in genomic DNA. Possible mechanisms for the processing of the legumin precursor are discussed. Identification of cloned cDNA sequences coding for vicilin, the secondary storage protein of Pisum sativum4, is also reported.
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