Evolution of seed storage globulins and cupin superfamily

  title={Evolution of seed storage globulins and cupin superfamily},
  author={Andrei D. Shutov and Irina Kakhovskaya},
  journal={Molecular Biology},
An extensive superfamily of cupins (clan cl09118) currently combines thousands of functionally and structurally diverse prokaryote and eukaryote proteins, which contain a β-barrel of antiparallel β-strands (cupin module). Possible ways of the formation of the cupin superfamily were suggested based on the comparison of primary and tertiary structures of proteins from several conserved families of cupins including seed storage globulins and plant oxalate oxydases (germins), and bacterial oxalate… Expand
Seed storage globulins: Origin and evolution of primary and higher order structures
It is found that limited proteolysis of soybean legumin and kidney bean vicilin in germinating seeds and in vitro leads to their regular changes, which initiate an extensive cleavage of storage globulin molecules by the one-by-one mechanism. Expand
New aspects of the molecular evolution of legumains, Asn-specific cysteine proteinases.
The molecular evolution of asparagine-specific cysteine proteinases from plants and animals was analyzed using newly available related amino acid sequences from lower eukaryotes, bacteria and Archaea to suggest that genuine legumains originate from prokaryote pro-legumains. Expand
Quantitative subproteomic analysis of germinating related changes in the scutellum oil bodies of Zea mays.
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β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
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Anionic Antimicrobial and Anticancer Peptides from Plants
It is now becoming clear that AAMPs participate in the innate immune response of plants and make a major contribution to the arsenal of defence toxins produced by these organisms to compensate for their lack of some defence mechanisms possessed by mammals. Expand
An Acyl Transfer Reaction Catalyzed by an Epimerase MarH
MarH, a small protein (129 amino acids) belonging to the cupin superfamily, was previously characterized as an epimerase involved in the (2S,3S)-β-methyltryptophan formation in the maremycinExpand
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Microbial Relatives of the Seed Storage Proteins of Higher Plants: Conservation of Structure and Diversification of Function during Evolution of the Cupin Superfamily
This review summarizes the recent discovery of the cupin superfamily of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Expand
A gene encoding a vicilin-like protein is specifically expressed in fern spores. Evolutionary pathway of seed storage globulins.
It is proposed that seed storage globulins of spermatophytes evolved from desiccation-related single-domain proteins of prokaryotes via a duplicated two-domain ancestor that is best represented by the extant fern spore-specific vicilin-like protein. Expand
Microbial Relatives of Seed Storage Proteins: Conservation of Motifs in a Functionally Diverse Superfamily of Enzymes
Ability to maintain cell viability during periods of dehydration in spores and seeds may relate to absolute conservation of residues involved in structure determination in plant storage proteins. Expand
Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi
It is reported that amino acid sequences of legumin and vicilin domains share statistically significant similarity to the germination-specific germins of wheat as well as to the spherulation-specific spherulins of myxomycetes. Expand
Origin and Evolution of Seed Storage Globulins
This chapter considers: what proteins have been recruited as a progenitor molecule and what are the principle evolutionary milestones to convert this progenitors into a seed storage globulin. Expand
Legumin-like and vicilin-like seed storage proteins: Evidence for a common single-domain ancestral gene
The comparison of the intron/exon pattern reveals that at least three out of five intron positions are precisely conserved between the genes of both protein families, further supporting the idea of a common evolutionary origin of recent legumin and vicilin encoding genes. Expand
Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer
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Evolution of functional diversity in the cupin superfamily.
This review discusses the advantages of this particular scaffold and provides an evolutionary analysis of 18 different subclasses within the cupin superfamily. Expand
Storage and mobilization as antagonistic functional constraints on seed storage globulin evolution.
The evolved system of controlled structure-function interplay between storage globulins and proteinases is part of a syndrome that comprises differential compartmentation and gene expression of storage proteins andproteinases for controlling the total spatial and temporal patterns of globulin storage and mobilization in maturing and germinating seeds. Expand
Crystal structure of soybean proglycinin A1aB1b homotrimer.
The crystal structure of proglycinin is similar to those of canavalin and phaseolin belonging to the 7 S globulin family, strongly supporting the hypothesis that both 7 S and 11 S globulins are derived from a common ancestor. Expand