Evidence that the N-terminal extension of the Vicieae convicilin genes evolved by intragenic duplications and trinucleotide expansions

Genome ◽  
2001 ◽  
Vol 44 (6) ◽  
pp. 1022-1030 ◽  
Author(s):  
L E Sáenz de Miera ◽  
M Pérez de la Vega
Keyword(s):  
Amino Acids ◽  
Lens Culinaris ◽  
Storage Proteins ◽  
Phylogenetic Analyses ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Plant Seed ◽  
Vicilin Gene

This study was aimed to identify lentil (Lens culinaris subsp. culinaris) convicilin genes and to carry out a comparative analysis of these genes in the tribe Vicieae. Convicilins differ from vicilins, a related group of plant seed storage proteins, mainly by the presence of an additional sequence of amino acids in the sequence corresponding to the first exon, referred as the N-terminal extension. A single gene for convicilin, a component of legume seed storage proteins, was identified in the cultivated lentil. In this species, the N-terminal extension is formed by a stretch of 126 amino acids of which 59.2% are charged amino acids: 29.6% glutamic acid, 3.2% aspartic acid, 14.4% arginine, 8.8% lysine, and 3.2% histidine. This lentil convicilin sequence is similar to the sequence of convicilins in other species of the tribe Vicieae. However, the size of the N-terminal extension clearly differs among convicilins. Sequence comparison and phylogenetic analyses including convicilin and vicilin of Vicieae species indicated that the differentiation between vicilins and convicilins predated the differentiation of the two vicilin gene families (47- and 50-kDa vicilins), and that the N-terminal extension evolved mainly by a series of duplications of short internal sequences and triplet expansions, the predominant one being GAA.Key words: convicilin, evolution by duplications, Lens culinaris Medik., lentil, legumes, trinucleotide expansion.

Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded ω-type prolamin sequence from wheat

Genome ◽  
2002 ◽  
Vol 45 (4) ◽  
pp. 661-669 ◽  
Author(s):  
Ali Masoudi-Nejad ◽  
Shuhei Nasuda ◽  
Akira Kawabe ◽  
Takashi R Endo
Keyword(s):  
Storage Proteins ◽  
Protein Structures ◽  
Seed Storage ◽  
Chromosome Mapping ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
Start Codon ◽  
Pcr Analysis ◽  
Bread Making ◽  
Deletion Lines

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the α-, β-, γ-, and ω-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an ω-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the ω-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the ω-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the α- and β-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the ω-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The ω-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the ω-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-A1a in 'Chinese Spring'.Key words: glutenin, omega gliadin, storage protein, Triticum aestivum, secalin.

Protamine sulfate precipitation method depletes abundant plant seed-storage proteins: A case study on legume plants

PROTEOMICS ◽  
2015 ◽  
Vol 15 (10) ◽  
pp. 1760-1764 ◽  
Author(s):  
Yu Ji Kim ◽  
Yiming Wang ◽  
Ravi Gupta ◽  
So Wun Kim ◽  
Chul Woo Min ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protamine Sulfate ◽  
Precipitation Method ◽  
Plant Seed ◽  
Legume Plants

A comparative study of convicilin storage protein gene sequences in species of the tribe Vicieae

Genome ◽  
2008 ◽  
Vol 51 (7) ◽  
pp. 511-523 ◽  
Author(s):  
L. E. Sáenz de Miera ◽  
J. Ramos ◽  
M. Pérez de la Vega
Keyword(s):  
Amino Acids ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Sequences ◽  
Replication Slippage ◽  
Charged Amino Acids ◽  
Arginine Residues ◽  
Related Group ◽  
Additional Sequence

Convicilins, a set of seed storage proteins, differ from vicilins, a related group of seed storage proteins, mainly because of the presence of the N-terminal extension, an additional sequence of amino acids in the sequence corresponding to the first exon. Convicilins have been described only in species of the legume tribe Vicieae. One or two genes for convicilins have been identified in most species of this tribe. The genus Pisum is the main exception, since two genes have been identified in most of its species. Thirty-four new convicilin gene sequences from 29 different species ( Lathyrus , Lens , Pisum, and Vicia spp.) have been analyzed here. Convicilin gene sequences are generally organized in 6 exons, but in some instances one of the internal introns (2nd or 4th) is lost. In these 29 species, the N-terminal extension is formed by a stretch of 99 to 196 amino acids particularly rich in polar and charged amino acids (on average, it contains 29.43% glutamic acid and 15.38% arginine residues). This N-terminal extension has the characteristics of an intrinsically unstructured region (IUR), one of the categories of protein “degenerate sequences”. A comparative analysis indicates that the N-terminal extension sequence has evolved faster than the surrounding sequence, which is common to all vicilins, and it evolved mainly through a series of duplications of short internal sequences and triplet expansions, the predominant one being GAA. This agrees with the evolution of IURs, which is faster than the evolution of surrounding sequences and is mainly due to replication slippage and unequal crossover recombination. Alternative maximum-likelihood trees of phylogenetic relationships among the 29 Vicieae species based on the convicilin exon sequences are presented and discussed.

scholarly journals Development of reduced gluten wheat enabled by determination of the genetic basis of thelys3alow hordein barley mutant

2018 ◽  
Author(s):  
Charles P. Moehs ◽  
William J. Austill ◽  
Aaron Holm ◽  
Tao A. G. Large ◽  
Dayna Loeffler ◽  
...  
Keyword(s):  
Celiac Disease ◽  
Storage Proteins ◽  
Single Gene ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Nucleotide Polymorphisms ◽  
Related Condition ◽  
Single Nucleotide ◽  
Wheat Gene

AbstractCeliac disease is the most common food-induced enteropathy in humans with a prevalence of approximately 1% world-wide [1]. It is induced by digestion-resistant, proline- and glutamine-rich seed storage proteins, collectively referred to as “gluten,” found in wheat. Related prolamins are present in barley and rye. Both celiac disease and a related condition called non-celiac gluten sensitivity (NCGS) are increasing in incidence [2] [3]. This has prompted efforts to identify methods of lowering gluten in wheat, one of the most important cereal crops. Here we used BSR-seq (Bulked Segregant RNA-seq) and map-based cloning to identify the genetic lesion underlying a recessive, low prolamin mutation (lys3a) in diploid barley. We confirmed the mutant identity by complementing thelys3amutant with a transgenic copy of the wild type barley gene and then used TILLING (Targeting Induced Local Lesions in Genomes) [4] to identify induced SNPs (Single Nucleotide Polymorphisms) in the three homoeologs of the corresponding wheat gene. Combining inactivating mutations in the three sub-genomes of hexaploid bread wheat in a single wheat line lowered gliadin and low molecular weight glutenin accumulation by 50-60% and increased free and protein-bound lysine by 33%. This is the first report of the combination of mutations in homoeologs of a single gene that reduces gluten in wheat.

Gene Families Encoding Isoforms of Two Major Sesame Seed Storage Proteins, 11S Globulin and 2S Albumin†

2006 ◽  
Vol 54 (25) ◽  
pp. 9544-9550 ◽  
Author(s):  
Eric S. L. Hsiao ◽  
Li-Jen Lin ◽  
Feng-Yin Li ◽  
Miki M. C. Wang ◽  
Ming-Yuan Liao ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Gene Families ◽  
2S Albumin ◽  
11S Globulin
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