Developmental biochemistry of cottonseed embryogenesis and germination XVIII cDNA and amino acid sequences of members of the storage protein families

Chlan, Caryl A.; Pyle, J. B.; Legocki, Andrzej B.; Dure, Leon S.

doi:10.1007/bf00020331

Cited by 69 publications

(51 citation statements)

References 20 publications

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“…In agreement with prior research, which characterized the two principal forms of vicilin as occurring at 48 kDa and 52 kDa (Dure and Chlan 1981;Chlan et al 1986), these vicilin isoforms were also observed as the most abundant proteins on our proteomic maps. Their relative abundances (37% in the AD genome, 36% in the A genome, and 28% in the D genome), however, were a little higher than the previous estimate of 27% by cylindrical SDS-PAGE (Dure and Chlan 1981).…”

Section: Discussionsupporting

confidence: 92%

“…Because mature albumins are typically cleaved into smaller polypeptides that fall outside of the effective separation range of SDS-PAGE, we cannot rule out the possibility that the poor representation of albumin in the present protein profiles may be due to a technical limitation of 2-DE profiling; however, other estimates of protein abundances, which rely on amino acid composition, concur with our assessment. That is, cotton seeds have been characterized as deficient in sulfur-containing amino acids, indicating that sulfur-rich proteins (such as albumin) constitute a low fraction of the total seed proteins (Bressani et al 1966;Chlan et al 1986;Galau et al 1991Galau et al , 1992.…”

Section: Discussionmentioning

confidence: 99%

“…The major Gossypium SSPs have previously been characterized (Dure and Chlan 1981;Galau et al 1983;Chlan et al 1986Chlan et al , 1987Dure 1989;Galau et al 1991), although complete gene sequences were limited to G. hirsutum. In surveying the Gossypium EST databases, a considerable level of nucleotide diversity became evident, not only for the orthologous genes obtained from the diploid species, but also for copies found in the G. hirsutum EST database.…”

Section: Genetic Analysis Of Gossypium Ssp Genesmentioning

confidence: 99%

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Genomically Biased Accumulation of Seed Storage Proteins in Allopolyploid Cotton

Houston

Pathak

et al. 2011

Genetics

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Allopolyploidy is an important process during plant evolution that results in the reunion of two divergent genomes into a common nucleus. Many of the immediate as well as longer-term genomic and epigenetic responses to polyploidy have become appreciated. To investigate the modifications of gene expression at the proteome level caused by allopolyploid formation, we conducted a comparative analysis of cotton seed proteomes from the allopolyploid Gossypium hirsutum (AD genome) and its model Agenome and D-genome diploid progenitors. An unexpectedly high level of divergence among the three proteomes was found, with about one-third of all protein forms being genome specific. Comparative analysis showed that there is a higher degree of proteomic similarity between the allopolyploid and its D-genome donor than its A-genome donor, reflecting a biased accumulation of seed proteins in the allopolyploid. Protein identification and genetic characterization of high-abundance proteins revealed that two classes of seed storage proteins, vicilins and legumins, compose the major component of cotton seed proteomes. Analyses further indicate differential regulation or modification of homoeologous gene products, as well as novel patterns in the polyploid proteome that may result from the interaction between homoeologous gene products. Our findings demonstrate that genomic merger and doubling have consequences that extend beyond the transcriptome into the realm of the proteome and that unequal expression of proteins from diploid parental genomes may occur in allopolyploids.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Genetic Analysis Of Gossypium Ssp Genesmentioning

confidence: 99%

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Genomically Biased Accumulation of Seed Storage Proteins in Allopolyploid Cotton

Houston

Pathak

et al. 2011

Genetics

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“…Sequence d a t a from a non-legA c D N A clone o f Pisum (with a b o u t 42% a m i n o acid sequence identity to legA) and o f two legumin genes from Viciafaba, also indicates a similar glutamic acid and aspartic acid-rich region[12,40]. In addition, the h o m o l o g o u s cotton genes described by Chlan et al[7] also contain such a region. Large insertions and deletions o f the types seen in the ot peptide are not seen in the/3 peptidecoding p o r t i o n s o f the genes compared.…”

mentioning

confidence: 98%

Molecular cloning, genomic organization, expression and evolution of 12S seed storage protein genes of Arabidopsis thaliana

1988

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We have identified a number of genes of the flowering plant Arabidopsis thaliana that are abundantly expressed during embryogenesis. In this paper we discuss four of these genes, which comprise a gene family: complete genomic nucleotide sequence of two of the genes and partial sequence of the other two shows that they are all homologous to the 12S globulin seed storage protein genes of other angiosperms. The four genes fall into three subfamilies, as defined by cross-hybridization. One subfamily contains two genes in the Landsberg erecta strain, but only a single gene in the Columbia strain of Arabidopsis. The other two of these 12S gene subfamilies contain only single genes in both strains. Thus, the seed storage protein gene family in Arabidopsis appears much simpler than that in other higher plants.These genes are expressed during the latter half of embryogenesis, a period in which abscisic acid (ABA) is thought to play a role in gene regulation, and known to play a role in seed physiology. We observed no significant difference in the expression profiles of these four genes in ABA-deficient and ABA-insensitive mutants of Arabidopsis, except that the onset of detectable expression of all of the transcripts is slightly delayed in both types of mutants.

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“…6. The deduced amino acid sequence of pumpkin preproglobulin was compared with those of precursor proteins of soybean glycinin [25], pea legumin [27], cotton /3 globulin [31] and rape 11-S globulin [32] (Fig. 7).…”

Section: Resultsmentioning

confidence: 99%

Nucleotide sequence of cloned cDNA coding for pumpkin 11‐S globulin β subunit

Hayashi

Mori

Nishimura

et al. 1988

European Journal of Biochemistry

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cDNA coding for preproglobulin β, a precursor protein of 11‐S globulin β subunit, was cloned and the nucleotide sequence has been determined. The sequence covers the whole coding region (1440 base pairs) with 5′ and 3′ noncoding region (30 and 214 base pairs, respectively). The deduced amino acid sequence of preproglobulin β consists of a 21‐amino‐acid N‐terminal signal peptide, preceding the acidic γ polypeptide region (275 amino acids) and the subsequent basic δ region (184 amino acids). The site for post‐translational cleavage of the precursor polypeptide to make the γ and δ chains is estimated to be located between the asparagine‐glycine residues. The N‐terminal amino acid of the γ chain of mature 11‐S globulin β subunit was reported to be blocked by 5‐oxoproline (pyroglutamic acid) [Ohmiya et al. (1980) Plant Cell Physiol. 21, 157–1671. It was shown that the blocked N‐terminal amino acid is coded as a glutamine residue. The derived amino acid sequence was also compared with those of precursor proteins of other 11‐S globulins such as soybean glycinin, cotton β globulin, pea legumin and rape 11‐S globulin by dot matrix analysis.

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Developmental biochemistry of cottonseed embryogenesis and germination XVIII cDNA and amino acid sequences of members of the storage protein families

Cited by 69 publications

References 20 publications

Genomically Biased Accumulation of Seed Storage Proteins in Allopolyploid Cotton

Genomically Biased Accumulation of Seed Storage Proteins in Allopolyploid Cotton

Molecular cloning, genomic organization, expression and evolution of 12S seed storage protein genes of Arabidopsis thaliana

Nucleotide sequence of cloned cDNA coding for pumpkin 11‐S globulin β subunit

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