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Page 1 from 52 results
The mitochondrial processing peptidase from potato: a self-processing enzyme encoded by two differentially expressed genes.
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Cytochrome c reductase from potato is a bifunctional protein complex located in the inner mitochondrial membrane, which is involved in respiratory electron transport and processing of mitochondrial precursor proteins. The three largest subunits of the complex share the highest degree of sequence
Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria.
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In potato, cytochrome c reductase, a protein complex of the respiratory chain, exhibits processing activity toward mitochondrial precursor proteins. One of the two cooperating components of the processing peptidase was shown to be identical with subunit III of the complex. Here we report that two
The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.
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The major mitochondrial processing activity removing presequences from nuclear encoded precursor proteins is present in the soluble fraction of fungal and mammalian mitochondria. We found that in potato, this activity resides in the inner mitochondrial membrane. Surprisingly, the proteolytic
The Cytochrome c Reductase Integrated Processing Peptidase from Potato Mitochondria Belongs to a New Class of Metalloendoproteases.
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The general mitochondrial processing peptidase that removes the N-terminal targeting signals from proteins imported into mitochondria forms part of a respiratory protein complex in potato (Solanum tuberosum L.). We have termed this complex the "cytochrome c reductase/processing peptidase complex"
Two cDNA clones encoding isoforms of the beta-subunit of the general mitochondrial processing peptidase from potato.
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Cytochrome-c reductase/processing peptidase complex from potato mitochondria.
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Molecular features, processing and import of the Rieske iron-sulfur protein from potato mitochondria.
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The mitochondrial iron-sulfur protein (also termed Rieske iron-sulfur protein) of cytochrome c reductase was purified from potato tubers and identified with heterologous antibodies. The sequences of the N-terminus of this 25 kDa protein and of an internal peptide were determined to design
Characterization of Isolates of Phytophthora infestans from Tomato and Potato in North Carolina from 1993 to 1995.
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Eighty-five isolates of Phytophthora infestans from 33 tomato and 8 potato fields in North Carolina, South Carolina, and Tennessee were collected from 1993 to 1995 and tested for mating type, sensitivity to metalaxyl, and allozyme genotype at glucose-6-phosphate isomerase (Gpi) and peptidase (Pep)
Enzymatic generation of peptides from potato proteins by selected proteases and characterization of their structural properties.
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The use of low grade starting material for the generation of peptides with bioactivity properties is of interest. The proteins from the potato starch industry byproduct is a promising source, as several health benefits may be associated with their hydrolysates. The efficiency of selected proteases
Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network.
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The Colorado potato beetle (CPB), Leptinotarsa decemlineata, is a major pest of potato plants, and its digestive system is a promising target for development of pest control strategies. This work focuses on functional proteomic analysis of the digestive proteolytic enzymes expressed in the CPB gut.
Inhibition of cysteine proteinases by a protein inhibitor from potato.
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The inhibitory specificity of a protein from potato tubers that inhibits cysteine proteinases (potato cysteine proteinase inhibitor, PCPI) has been compared with that of chicken egg-white cystatin. Most proteinases that are inhibited by cystatin were also inhibited by PCPI, but the potato inhibitor
Characterization of atrial natriuretic peptide degradation by cell-surface peptidase activity on endothelial cells.
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Atrial natriuretic peptide (ANP) is a fluid-regulating peptide hormone that promotes vasorelaxation, natriuresis, and diuresis. The mechanisms for the release of ANP and for its clearance from the circulation play important roles in modulating its biological effects. Recently, we have reported that
P1 peptidase--a mysterious protein of family Potyviridae.
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The Potyviridae family, named after its type member, Potato virus Y (PVY), is the largest of the 65 plant virus groups and families currently recognized. The coding region for P1 peptidase is located at the very beginning of the viral genome of the family Potyviridae. Until recently P1 was thought
Genome-wide characterization, molecular evolution and expression profiling of the metacaspases in potato (Solanum tuberosum L.).
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Metacaspases are distant relatives of animal caspases found in plants, protozoa and fungi. Some recent studies have demonstrated that metacaspases are involved in regulating the developmental and environmentally induced programmed cell death in plants. In this study, we identified metacaspase gene
The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain.
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The bc1-complex (EC 1.10.2.2.) from Triticum aestivum L. was purified by cytochrome-c affinity chromatography and gel filtration using either etiolated seedlings or wheat-germ extract as starting material. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the isolated enzyme revealed ten
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