N‐terminal amino acid sequences of chloroform/methanol‐soluble proteins and albumins from endosperms of wheat, barley and related species

Shewry, Peter R.; Lafiandra, D.; Salcedo, Gabriel; Aragoncillo, Cipriano; Garcı́a-Olmedo, Francisco; Lew, Ellen J-L.; Dietler, Mary D.; Kasarda, Donald D.

doi:10.1016/0014-5793(84)80768-1

Cited by 63 publications

(40 citation statements)

References 29 publications

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“…2. tetrameric inhibitors, fully confirm that indeed the three proteins are members of the same protein family as the monomeric and dimeric a-amylase inhibitors, the trypsin inhibitors and the bifunctional inhibitors from cereals [2,3,11,34,35,37]. The sequences of subunits CM1, CM16, CM3 and CMd are closer to each other (47-86% identical residues) than to any of the other proteins in Fig.…”

Section: P G C P R Ti V Fojm Fo" F V Rl I |L V|t|p G| Y |C N L| T Plsupporting

confidence: 66%

“…Nucleotide sequences and deduced amino acid sequences of inserts in clones pCTl, pCT2, and pCT3, which respectively correspond to subunits CM3, CMl, and CM16 of the wheat tetrameric a-amylase inhibitor (indicated in parenthesis). Sequences identical to known N-terminal sequences of proteins CM3B [37] CMl and CMl 6 [2] are boxed. The AATAAA polyadenilation signáis are underlined.…”

Section: Chromosomal Locations Of Genesmentioning

confidence: 99%

“…The last type of subunit, two copies of which seem to be present in the tetramer, it also encoded in group 4 chromosomes, but the assignment was only tentative in the case of wheat, because proteins CM3B and CM3D could not be separated from each other by electrophoresis or by high-performance liquid chromatography [1,8,32]. Only N-terminal amino acid sequences have been determined for all these proteins [2,3,37], with the exception of protein CMd, for which the complete sequence has been deduced from the cloned cDNA [12,29]. We have now characterized cDNA clones corresponding to the three types of subunits in wheat and present evidence that the genes corresponding to proteins CM3B and CM3D are within a few kb from those encoding proteins CM16 and CM17, respectively, in chromosomes 4B and 4D.…”

Section: Introductionmentioning

confidence: 99%

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Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect ?-amylase

Garcı́a-Maroto¹,

Maraña²,

Mena

et al. 1990

Plant Mol Biol

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We have characterized three cDNA clones corresponding to proteins CM1, CM3 and CM16, which represent the three types of subunits of the wheat tetrameric inhibitor of insect a-amylases. The deduced amino acid sequences of the mature polypeptides are homologous to those of the dimeric and monomeric a-amylase inhibitors and of the trypsin inhibitors. The mature polypeptides are preceded by typical signal peptides. Southern blot analysis of appropriate aneuploids, using the cloned cDNAs as probes, has revealed the location of genes for subunits of the CM3 and of the CM16 type within a few kb of each other in chromosomes 4A, 4B and 4D, and those for the CM1 type of subunit in chromosomes 7A, 7B and 7D. Known subunits of the tetrameric inhibitor corresponding to genes from the B and D genomes have been previously characterized. No proteins of this class have been found to be encoded by the A genome in hexaploid wheat (genomes AA, BB, DD) or in diploid wheats (AA) and no anti a-amylase activity has been detected in the latter, so that the A-genome genes must be either silent (pseudogenes) or expressed at a much lower level.

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Section: P G C P R Ti V Fojm Fo" F V Rl I |L V|t|p G| Y |C N L| T Plsupporting

confidence: 66%

Section: Chromosomal Locations Of Genesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect ?-amylase

Garcı́a-Maroto¹,

Maraña²,

Mena

et al. 1990

Plant Mol Biol

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“…Thus it appears that the 2s Kunitz-type proteins and the 7 s and 12s globulins constitute a wider family of related proteins which may have evolved from a common ancestral precursor either by a process of gene duplication or exon deletion to produce the genes found today. This protein family, however, is distinct from the seed protein superfainily [29] which is characterized by the conservation of the number and positions of the cysteine residues and includes 2s albumins of wheat and inhibitors of trypsin and a-amylase from cereals, and 2s proteins of castor bean and rapeseed. In summary, the primary structure of the major seed albumin of winged bean seed has shown that it is related to the 2s Kunitz-type seed inhibitors and that this family of 2s proteins is related to the storage globulins found in many seeds.…”

Section: Resultsmentioning

confidence: 99%

Amino acid sequence of a crystalline seed albumin (winged bean albumin‐1) from Psophocarpus tetragonolobus (L.) DC

Kortt

Strike

Jersey

1989

European Journal of Biochemistry

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The complete amino acid sequence of winged bean albumin-1 (WBA-1) of Psophocarpus tetragonolobus (L.) DC has been determined. The protein consists of a single polypeptide chain of 175 amino acid residues, with one disulfide bond, corresponding to a molecular mass of 19333 Da. WBA-1 was found to be homologous with the Kunitz-type seed trypsin inhibitors. The similarity between WBA-1 and the trypsin inhibitors from soybean and winged bean was 38% and 28%, respectively; similarity was most marked in the C-terminal third of the sequence with identities of 47% and 37%, respectively. Significant similarity was found also between the 2s Kunitz-type proteins and the carboxy-terminal region of the 7s storage globulins, suggesting that these two groups of proteins are related and may have evolved from a common ancestral precursor. Circular dichroism measurements suggest a high content of p sheet (52%) while secondary structure predictions based on amino acid sequence indicate a similar content and distribution of p sheet to that found for soybean trypsin inhibitor by X-ray diffraction studies. A recent study [4] reported the purification of the major seed albumin, winged bean albumin-1 (WBA-l), which accounts for approximately 15% of the total seed protein. This albumin was observed to crystallize readily from solution during purification [4]. The isolation of a winged bean storage protein of similar size and crystalline form to WBA-1 has also been reported by Roy and Singh [S]. In a subsequent report [9] their protein preparation was shown to contain mainly the winged bean chymotrypsin inhibitor described previously [6] and not WBA-1. Preliminary amino acid sequence data of tryptic peptides derived from WBA-1 revealed partial sequence similarity with the 7s storage globulins vicilin, phaseolin and p-conglycinin suggesting a structural relationship between WBA-1 and the 7s class of seed globulins. WBA-1 has been crystallized in a form suitable for X-ray diffraction analysis and the three-dimensional structure of this seed protein is under investigation [lo]. Thus further sequence studies were deemed desirable to elucidate the relationship of WBA-1 to the 7s globulins and other 2s seed proteins. In this paper we report on the complete amino acid sequence of WBA-1 and on the relationship of this protein to the family of Kunitztype seed inhibitors and the 7 s globulins. EXPERIMENTAL PROCEDURESWinged bean albumin-1 (WBA-1) was isolated from mature seeds of Psophocarpus tetragonolobus variety Tpt-1 as described in [4]. The protein (20 mg) was reduced and alkylated with iodoacetic acid as described by Crestfield et al. [ll], dialysed extensively against distilled water and recovered by lyophilization. The S-carboxymethylated protein (50 nmol) in 1.0 ml 0.1 M ammonium bicarbonate buffer, pH 8.0, was digested at 37°C for 4 h with one of the following proteases [at an enzyme/substrate ratio of 1 : 50 (by mass)]: trypsin (Worthington), a-chymotrypsin (Worthington), Stuphylococcul aureus V8 protease (Pierce), endoproteinase Lys-C (B...

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“…Current evidence suggests that the cereal proteins of this type may belong to at least six distinct families. For example the a-amylase inhibitors from wheat [2][3][4], and rye [5], proteinase inhibitors from rye [5], barley [6] and maize [7], and a hifunctional a-amylase/trypsin inhibitor from ragi [8] belong to a so-called superfamily [9] which also includes the cereal chloroform-methanol (CM) soluble proteins and certain 2 S storage proteins from dicotyledonous plants. Other bifunctional inhibitors from barley [10,11], wheat [12,13] Correspondence address: M. Richardson, Department of Botany, University of Durham, Science Laboratories, South Road, Durham DHI 3LE, England and rice [14] have sequence homology with the legume Kunitz inhibitor family, while proteinase inhibitors from barley [15,16] clearly belong to the potato inhibitor 1 family.…”

Section: Introductionmentioning

confidence: 99%

The amino acid sequence of a cereal Bowman‐Birk type trypsin inhibitor from seeds of Jobs' tears (Coix lachryma‐jobi L.)

1988

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The major trypsin inhibitor from seeds of Jobs' tears (Coix lachryma-jobO was purified by heat treatment, fractional precipitation with (NH4)2SO4, ion-exchange chromatography on DEAE-Sepharose, gel-filtration on Sephadex G-75 and preparative reverse-phase HPLC. The complete amino acid sequence was determined by analysis of peptides derived from the reduced and S-carboxymethylated protein by digestion with trypsin, chymotrypsin and the S. aureus V8 protease. The polypeptide contained 64 amino acids with a high content of cysteine. The sequence exhibited strong homology with a number of Bowman-Birk inhibitors from legume seeds and similar proteins recently isolated from wheat and rice.

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N‐terminal amino acid sequences of chloroform/methanol‐soluble proteins and albumins from endosperms of wheat, barley and related species

Cited by 63 publications

References 29 publications

Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect ?-amylase

Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect ?-amylase

Amino acid sequence of a crystalline seed albumin (winged bean albumin‐1) from Psophocarpus tetragonolobus (L.) DC

The amino acid sequence of a cereal Bowman‐Birk type trypsin inhibitor from seeds of Jobs' tears (Coix lachryma‐jobi L.)

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