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A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins.

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Two types of cysteine proteases, low-specificity enzymes from the papain family and Asn-specific from the legumain family are generally considered to be the major endopeptidases responsible for the degradation of seed storage proteins during early seedling growth. The action of the corresponding

A distinct subfamily of papain-like cystein proteinases regulated by senescence and stresses in Glycine max.

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GMCP3 encodes a cystein proteinase of Glycine max belonging to the papain-like family (C1A in MEROPS database) that was previously found to be involved in the mobilization of protein reserves during seed germination. Here, we report that GMCP3 is induced by senescence and diverse stresses in

Role of cysteine proteinase inhibitors in preference of Japanese beetles (Popillia japonica) for soybean (Glycine max) leaves of different ages and grown under elevated CO2.

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Elevated levels of CO(2), equivalent to those projected to occur under global climate change scenarios, increase the susceptibility of soybean foliage to herbivores by down-regulating the expression of genes related to the defense hormones jasmonic acid and ethylene; these in turn decrease the gene

Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog.

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Diverse functions for three soybean (Glycine max L. Merr.) cysteine proteinase inhibitors (CysPIs) are inferred from unique characteristics of differential regulation of gene expression and inhibitory activities against specific Cys proteinases. Based on northern blot analyses, we found that the

[Cysteine proteinase inhibitors from soy seeds].

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Protein inhibitors of cysteine proteinases possessing unusual properties have been found in soya (Glycine max) seeds. One of the inhibitor forms has also been detected in Bowman-Birk inhibitor preparations (both commercial and purified by affinity chromatography on chymotrypsin-Sepharose ones). A

Cloning of two cysteine proteinase genes, CysP1 and CysP2, from soybean cotyledons by cDNA representational difference analysis.

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By cDNA representational difference analysis (cDNA RDA) and rapid amplification of cDNA ends (RACE), we isolated two cDNAs, CysP1 and CysP2, from the cotyledons of growing soybean (Glycine max (L.) Merr.) seedlings. CysP1 cDNA is 1265 bp in size with a 1089-bp open reading frame (ORF), and CysP2

Different Rates of Metabolism of Soybean Proteinase Inhibitors during Germination.

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During germination, the content of the major Bowman-Birk proteinase inhibitor (BB-E) in the cotyledons of soybean (Glycine max [L.] Merrill cv. Fiskeby V) seeds decreases, becoming a minor form by the sixth day of germination. One of the three other minor species (BB-D) of this inhibitor in the dry

cDNA cloning for a putative cysteine proteinase from developing seeds of soybean.

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cDNA clones for a putative cysteine proteinase were isolated from developing cotyledons of soybean (Glycine max.) using PCR-based techniques. The full-length clone of 1441 bp encodes a proteinase pre-propolypeptide of 380 amino acids. It belongs to the commonly known papain family and shows the

A novel Glycine soja cysteine proteinase inhibitor GsCPI14, interacting with the calcium/calmodulin-binding receptor-like kinase GsCBRLK, regulated plant tolerance to alkali stress.

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It has been well demonstrated that cystatins regulated plant stress tolerance through inhibiting the cysteine proteinase activity under environmental stress. However, there was limited information about the role of cystatins in plant alkali stress response, especially in wild soybean. Here, in this

Subtilisin inhibitor like protein 'ppLPI-1' from leaves of pigeonpea (Cajanus cajan, cv. BSMR 736) exhibits inhibition against Helicoverpa armigera gut proteinases.

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Helicoverpa armigera is an orthodox rival of many crop plants affecting agricultural economy. Plant leaves found to accumulate proteinase inhibitors, although this insect pest chooses leaves for laying eggs. Plant defense response at this juncture is not fully explored. In this context, here we are

Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression.

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We isolated and characterized two cDNAs for aspartic proteinases (APs; EC 3.4.23) in soybean [Glycine max (L.) Merr.]. The encoded enzymes, soyAP1 and soyAP2, share 55% amino acid sequence identity. Northern analysis demonstrated that soyAP1 is expressed specifically in seeds, especially in dry

RNA-Seq profiling of a defective seed coat mutation in Glycine max reveals differential expression of proline-rich and other cell wall protein transcripts.

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The plant cell wall performs a number of essential functions including providing shape to many different cell types and serving as a defense against potential pathogens. The net pattern mutation creates breaks in the seed coat of soybean (Glycine max) because of ruptured cell walls. Using RNA-Seq,

Population-specific gene expression in the plant pathogenic nematode Heterodera glycines exists prior to infection and during the onset of a resistant or susceptible reaction in the roots of the Glycine max genotype Peking.

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BACKGROUND A single Glycine max (soybean) genotype (Peking) reacts differently to two different populations of Heterodera glycines (soybean cyst nematode) within the first twelve hours of infection during resistant (R) and susceptible (S) reactions. This suggested that H. glycines has

[Effect of Cu and As and their combination pollution on Glycine max].

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Experiments are carried out with hoagland cultivation to study the effects of Cu and As and their interactions on the germination and seedling growth of Glycine max. The results show that Cu or As pollution reduced proteinase activities, inhibited the seedling growth and the respiration rate of

Purification and Developmental Analysis of an Extracellular Proteinase from Young Leaves of Soybean.

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A proteinase present in intercellular wash fluids from leaves of Glycine max has been purified 600-fold to electrophoretic homogeneity. The native protein is monomeric with a molecular mass of 60 kD, as estimated by denaturing gel electrophoresis, and has an isoelectric point of 7.7. The enzyme has

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