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cytochrome c/kartoffelplante
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Molecular structure of the 8.0 kDa subunit of cytochrome-c reductase from potato and its delta psi-dependent import into isolated mitochondria.
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The cytochrome-c reductase (EC 1.10.2.2) of the mitochondrial respiratory chain couples electron transport from ubiquinol to cytochrome c with proton translocation across the inner mitochondrial membrane. The enzyme from potato was shown to be composed of 10 subunits. Isolation and characterization
Primary structure, cell-free synthesis and mitochondrial targeting of the 8.2 kDa protein of cytochrome c reductase from potato.
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Cytochrome c reductase from potato comprises ten subunits with apparent molecular sizes between 55 and < 10 kDa. The subunit with the highest electrophoretic mobility on SDS-polyacrylamide gels was isolated and analysed by cyclic Edman degradation. Mixtures of degenerative oligonucleotides were
The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence.
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The 'Hinge' protein of cytochrome c reductase from fungi and mammals is thought to support electron transport from cytochrome c1 to cytochrome c and was reported to be one of the most acidic proteins known. Isolation and analysis of cDNA clones of the first 'Hinge' protein from a plant source
[Membrane lipids and electron transfer. Effects of four detergents on NADH-ferricyanide reductase and NADH-cytochrome c reductase activities of potato tuber microsomes].
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The NADH-ferricyanure reductase activity of Potato microsomes is stimulated by non ionic detergents (Triton X100 and Tween80) and is partially inhibited by ionic detergents (sodium-cholate and deoxycholate). All these four detergents progressively decreased the NADH-cytochrome c reductase in the
The nuclear gene for subunit Vc of sweet potato cytochrome c oxidase.
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We have cloned the gene for subunit Vc of sweet potato cytochrome c oxidase using its cDNA as a probe. There is a single intron, located one nucleotide upstream of the start of the open reading frame. No typical TATA-box sequence is present in the region upstream of the site of initiation of
Cytochrome c oxidase mRNA as an internal control for detection of Potato virus Y and Potato leafroll virus from single aphids by a co-amplification RT-PCR assay.
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Using cytochrome c oxidase subunit 1 (COX1) mRNA as the internal control, a triplex reverse transcription-polymerase chain reaction (RT-PCR) for detection of Potato virus Y (PVY) and Potato leafroll virus (PLRV) with co-amplification of COX1 from single specimens of various aphid species has been
Molecular features and mitochondrial import pathway of the 14-kilodalton subunit of cytochrome c reductase from potato.
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The cytochrome c reductase complexes from fungi and mammals both contain a 14-kD protein (yeast, 14.4 kD; bovine, 13.4 kD) that does not directly participate in electron transfer but possibly is indirectly involved in the function of the complex and has a role in assembly of the multimeric enzyme. A
Separation, amino-terminal sequence and cell-free synthesis of the smallest subunit of sweet potato cytochrome c oxidase.
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The smallest subunit (V) of sweet potato cytochrome c oxidase was separated into three polypeptides, Va, Vb and Vc with different molecular masses (7.4 kDa, 6.8 kDa and 6.2 kDa respectively) by highly resolving sodium dodecylsulfate polyacrylamide gel electrophoresis. Antibody against subunit V
Ubiquinol-cytochrome c oxidoreductase of higher plants. Isolation and characterization of the bc1 complex from potato tuber mitochondria.
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A procedure is described for isolation of active ubiquinol-cytochrome c oxidoreductase (bc1 complex) from potato tuber mitochondria using dodecyl maltoside extraction and ion exchange chromatography. The same procedure works well with mitochondria from red beet and sweet potato. The potato complex
Mechanism of increase in cytochrome c oxidase activity in sweet potato root tissue during aging of slices.
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The mechanism of an increase in cytochrome c oxidase [EC 1.9.3.1] activity during aging of sliced sweet potato root tissue was investigated with antibiotics and antibody to the purified enzyme. 1. The increase in cytochrome c oxidase activity was inhibited by chloramphenicol but not by
Molecular cloning of a cDNA for the smallest nuclear-encoded subunit of sweet potato cytochrome c oxidase. Analysis with the cDNA of the structure and import into mitochondria of the subunit.
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A cDNA clone for the subunit Vc, the smallest nuclear-encoded subunit, of sweet potato cytochrome c oxidase was isolated. Nucleotide sequence analysis showed that the subunit is synthesized as a precursor from which only the amino-terminal amino acid, methionine, residue is removed to form the
Presence of an inactive protein immunologically analogous to cytochrome c oxidase in the inner membrane of sweet potato root mitochondria.
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A protein, which was immunoreactive to antibody against cytochrome c oxidase, was found in the mitochondrial membrane fraction of sweet potato root tissue. The protein was associated relatively weakly with the mitochondrial inner membrane as compared with cytochrome c oxidase. It exerted no
Cytochrome c dependent, antimycin-A resistant respiration in mitochondria from potato tuber (Solanum tuberosum L.). Influence of wounding and storage time on outer membrane NADH-cytochrome-c-reductase.
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Cytochrome c has two stimulatory effects on respiration of mitochondria especially those from wounded potato tuber. In the first place a stimulation of succinate- and NADH-consuming, antimycin-A-sensitive respiration, which reaches a maximal value at low cytochrome c concentrations, has been found.
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
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