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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
Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill].
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The enzymatic properties of novel cysteine proteases D3-alpha and beta which were purified from germinating soybean cotyledons were investigated. The enzyme activities were exhibited in the presence of a thiol reagent, such as 2-mercaptoethanol, and apparently inhibited by E-64, a cysteine protease
Refined glufosinate selection in Agrobacterium-mediated transformation of soybean [Glycine max (L.) Merrill].
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Modern genetic analysis and manipulation of soybean ( Glycine max) depend heavily on an efficient and dependable transformation process, especially in public genotypes from which expressed sequence tag (EST), bacterial artificial chromosome and microarray data have been derived. Williams 82 is the
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
In silico and in vitro characterization of phospholipase A₂ isoforms from soybean (Glycine max).
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At the present, no secreted phospholipase A₂ (sPLA₂) from soybean (Glycine max) was investigated in detail. In this work we identified five sequences of putative secreted sPLA₂ from soybean after a BLAST search in G. max database. Sequence analysis showed a conserved PA2c domain bearing the Ca²⁺
[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
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
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
Survey of the Proteolytic Activities Degrading the Kunitz Trypsin Inhibitor and Glycinin in Germinating Soybeans (Glycine max).
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The cotyledons of the soybean (Glycine max [L.] Merrill cv Amsoy 71) were examined for proteolytic activities capable of degrading soybean seed proteins. Three distinct activities were identified that attack the native Kunitz soybean trypsin inhibitor of Amsoy 71, Ti(a). Protease K1 cleaves Ti(a) to
Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease.
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Protease K1 activity initiates the degradation of the Kunitz soybean trypsin inhibitor (KSTI) during germination and early seedling growth. This enzyme was purified nearly 1300-fold from the cotyledons of 4-day-old soybean (Glycine max [L.] Merrill) seedlings. Protease K1 is a cysteine protease with
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
Protease C2, a cysteine endopeptidase involved in the continuing mobilization of soybean beta-conglycinin seed proteins.
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The protease that degrades the beta subunit of the soybean (Glycine max (L.) Merrill) storage protein beta-conglycinin was purified from the cotyledons of seedlings grown for 12 days. The enzyme was named protease C2 because it is the second enzyme to cleave the beta-conglycinin storage protein, 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
Transcriptional profiling reveals elevated CO2 and elevated O3 alter resistance of soybean (Glycine max) to Japanese beetles (Popillia japonica).
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The accumulation of CO2 and O3 in the troposphere alters phytochemistry which in turn influences the interactions between plants and insects. Using microarray analysis of field-grown soybean (Glycine max), we found that the number of transcripts in the leaves affected by herbivory by Japanese
Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1.
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We have isolated a novel human cDNA encoding a protein of 433 amino acids which shows 40% sequence identity to a hemoglobinase of Schistosoma japonicum, one of the cysteine proteases in the pathway by which trematodes degrade host-cell globin. It also has 36% identity to a cysteine protease of the
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