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proteinase/nicotiana

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Sulfhydryl-endopeptidase (SH-EP) is a papain-type vacuolar proteinase expressed in cotyledons of germinated Vigna mungo seeds, and the enzyme possesses a C-terminal propeptide containing KDEL tail, an endoplasmic reticulum retention signal for soluble proteins. SH-EP is transported to vacuoles via a
A member of the potato proteinase inhibitor II (PPI-II) gene family under the control of the cauliflower mosaic virus 35S promoter has been introduced into tobacco (Nicotiana tabacum). Purification of the PPI-II protein that accumulates in transgenic tobacco has confirmed that the N-terminal signal
Coinfection of Nicotiana benthamiana with Potato virus A (PVA, a potyvirus) and Potato leaf-roll virus (PLRV, a luteovirus) induces a synergistic interaction manifested by enhanced titers of PLRV. The helper component proteinase (HC-Pro) of potyviruses is involved in viral vascular movement and

Inhibition of Sucrose Enhancer Effect of the Potato Proteinase Inhibitor II Promoter by Salicylic Acid.

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Effect of salicylic acid (SA) on the expression of the potato proteinase inhibitor (PI) II promoter was studied with transgenic tobacco plants (Nicotiana tabacum) carrying a gene fusion between the PI-II promoter and the chloramphenicol acetyltransferase (cat) reporter. As previously observed, the

Heterologous Expression of PKPI and Pin1 Proteinase Inhibitors Enhances Plant Fitness and Broad-Spectrum Resistance to Biotic Threats

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Kunitz-type (PKPI) and Potato type I (Pin1) protease inhibitors (PIs) are two families of serine proteinase inhibitors often associated to plant storage organs and with well known insecticidal and nematicidal activities. Noteworthy, their ability to limit fungal and bacterial pathogenesis in

Structure and induction pattern of a novel proteinase inhibitor class II gene of tobacco.

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A cDNA and a corresponding genomic clone encoding a protein with partial identity to type II proteinase inhibitors from potato, tomato and Nicotiana alata, were isolated from tobacco libraries. The protein of 197 amino acids contains a putative signal peptide of 24 residues and three homologous

Improved silencing suppression and enhanced heterologous protein expression are achieved using an engineered viral helper component proteinase.

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RNA silencing limits transient expression of heterologous proteins in plants. Co-expression of viral silencing suppressor proteins can increase and prolong protein expression, but highly efficient silencing suppressors may stress plant tissue and be detrimental to protein yields. Little is known

Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata.

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Proteinase inhibitors (PIs) of the potato type II family have been identified in a number of solanaceous species. Most family members have two PI domains which are specific for either chymotrypsin or trypsin. More recently family members have been described with three or six repeated PI domains.

Structural refinement of insecticidal plant proteinase inhibitors from Nicotiana alata.

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Ornamental tobacco (Nicotiana alata) produces a series of 6 kDa proteinase inhibitors belonging to the potato type II inhibitor family. These proteins inhibit trypsin and chymotrypsin, the main digestive enzymes of predatory insects, thus leading to starvation, impaired larval development or death.

Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors.

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A cDNA clone, NA-PI-II, encoding a protein with partial identity to proteinase inhibitor (PI) II of potato and tomato has been isolated from a cDNA library constructed from Nicotiana alata stigma and style mRNA. The cDNA encodes a polypeptide of 397 amino acids with a putative signal peptide of 29

cDNA cloning and gene expression analysis of the microbial proteinase inhibitor of tobacco.

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Tobacco mosaic virus-infected tobacco (Nicotiana tabacum var. Samsun NN) leaves produce a serine proteinase inhibitor that has evolved a specificity for microbial proteinases. We have isolated two closely related cDNAs that were shown to encode two active inhibitors. Southern analysis of genomic

Subcellular location of the helper component-proteinase of Cowpea aphid-borne mosaic virus.

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The helper component-proteinase (HC-Pro) of Cowpea aphid-borne mosaic virus (CABMV) was expressed in Escherichia coli and used to obtain HC-Pro antiserum that was used as an analytical tool for HC-Pro studies. The antiserum was used in immunofluorescence assays to study the subcellular location of

The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity.

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The cysteine protease CP14 has been identified as a central component of a molecular module regulating programmed cell death in plant embryos. CP14 belongs to a distinct subfamily of papain-like cysteine proteinases of which no representative has been characterized thoroughly to date. However, it

Differential accumulation of proteinase inhibitor I in normal and crown gall tissue of tobacco, tomato, and potato.

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A proteinase inhibitor (inhibitor I) is induced in crown gall tumors of tobacco (Nicotiana tabacum) initiated through infection with the tumorinducing bacterium, Agrobacterium tumefaciens, strains B6 or CG-14. Uninfected tissues do not contain immunologically detectable quantities of inhibitor I.

The Helper Component-Proteinase of Sweet potato feathery mottle virus Facilitates Systemic Spread of Potato virus X in Ipomoea nil.

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ABSTRACT When Ipomoea nil was coinfected with Sweet potato feathery mottle virus (SPFMV), a member of the genus Potyvirus, and Potato virus X (PVX) typical symptoms caused by PVX were observed on those by SPFMV on the first upper true leaves at 14 days postinoculation (dpi). On the other hand, no
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