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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 20 (1991), S. 405-410 
    ISSN: 1432-0983
    Keywords: ADP/ATP translocator ; Mitochondria ; Presequence ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ADP/ATP translocator is an abundant protein of the mitochondrial inner membrane, which in fungi and mammals is synthesized without a presequence. Here we report that the translocator from potato has an amino-terminal extension which may function in mitochondrial targeting. Several cDNA clones encoding the nucleotide sequence of the ADP/ATP translocator have been isolated from potato leaf and tuber cDNA libraries constructed in lambda phages. Only one class of cDNA clones was found but possibly different translocator genes are expressed in other tissues. High levels of transcripts for the translocator are found in all tissues analysed. Sequence determination of the complete insert of one of the clones reveals a long open reading frame of 1158 bp encoding a protein of 386 amino acids corresponding to a calculated molecular weight of 42 kDa. In contrast, the ADP/ATP translocator proteins from fungi and mammals are significantly smaller. Comparison of the Neurospora translocator with the potato protein shows about 75% sequence homology, being confined to the region after amino acid 85 of the potato polypeptide. Antibodies directed against the fungal translocator recognize a protein of 30 kDa in the inner membrane of potato mitochondria, suggesting that the mature protein has a similar size as the translocators from fungi and mammals. Thus, the additional segment of the potato ADP/ATP translocator forms an amino-terminal extension which may be involved in the import of the protein into plant mitochondria.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Stimulus transduction ; Bursting ; Temperature dependence ; Calcium entry blockers ; Siluriformes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Spontaneous afferent activity was recorded from 26 single ampullary electroreceptive organs of freshwater catfish (Ictalurus nebulosus LeS) at various temperatures. Regular grouping of action potentials was apparent in this secondary sensory system at 35°C and occasionally at 30°C. Impulse groups consisted of up to seven impulses. The precise timing of impulse generation and the temporal sequence of impulses indicated that oscillating processes are involved. Expectation density functions were calculated for records of afferent activity obtained at various temperatures below 35°C. In the majority of records the function was periodic. Impulse grouping and expectation density functions became more distinct in units exhibiting extremely high thresholds (i.e. being insensitive) to electrical stimuli. The results suggest that the oscillations originate from the postsynaptic membrane. The temporal pattern of impulse generation within impulse groups of ampullary electroreceptor organs and of specific warm and cold receptors was compared and found to be similar. Application of cadmium and menthol, which both reduce calcium entry, suppressed spontaneous activity in normal and insensitive electroreceptor systems, attenuated the sensitivity of normal receptors and modified the periodic pattern. This indicates that calcium is implicated in sensory transduction and in postsynaptic mechanisms. The data suggest that an oscillating process is one component of signal transmission in ampullary electroreceptor organs of teleost fish.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2013
    Keywords: Catfish ; Ampullary electroreceptors ; Stimulus transduction ; Temperature dependence ; Calcium channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The response properties of ampullary electroreceptors have been studied in the catfish Ictalurus nebulosus at skin temperatures between 5 and 35 °C. A unimodal relationship between spontaneous activity and temperature was obtained. Mean (±SEM) peak discharge rate was 57.3 ±1.8 impulses s−1 at 25 ° C; the receptors were active at 5 °C (15.0 impulses s−1) and at 35 °C (31.5 impulses s−1). There were no dynamic responses to temperature changes in either the warming or cooling direction. The shape of the frequency characteristic depended on temperature: the peak of the gain curve shifted to low frequencies at low temperatures. There was a concomitant change of the phase characteristic: the intersection at zero degree phase angle shifted to higher frequencies with an increase of temperature, thus increasing the lead at lower frequencies and decreasing the lag at higher frequencies. Latency after combined excitatory and inhibitory impulse stimulation was temperature dependent, ranging from 16.4 ms (5 °C) to 5.6 ms (35 °C). Application of the specific calcium channel blocker menthol (0.2 mM) suppressed spontaneous activity, the effect becoming more prominent at higher temperatures. Sensitivity to sinusoidal electrical stimulation was also impaired, but to a lesser degree and mainly at lower temperatures. We conclude that the filter properties of the receptor organ can be modelled by a band-pass filter in series with a latency, both of which are temperature dependent. These filter properties might be partially based on the activation kinetics of the tranduction channels.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Keywords: Cytochrome c 1 ; Solanum tuberosum ; Mitochondria ; Protein import ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Here we report the primary structure of potato cytochrome c 1, a nuclear-encoded subunit of complex III. Using heterologous antibodies directed against cytochrome c 1 from yeast two types of clones were isolated from an expression library, suggesting that at least two different genes are present and expressed in the genome. Northern blot analysis reveals that slightly varying levels of cytochrome c 1 transcripts are present in all potato tissues analysed. A 1304 bp insert of one of the cDNA clones (pC13II) encodes the entire 320 amino acids of the precursor protein corresponding to a molecular weight of 35.2 kDa. As revealed by direct amino acid sequence determination of the cytochrome c 1 protein another cDNA clone (pC18I) encodes the major form of cytochrome c 1 present in potato tuber mitochondria. Western blots of subfractionated potato mitochondria show that the mature protein present in the membrane fraction is smaller than the pC13II encoded protein synthesized in Escherichia coli. The transient presequence of the protein is 77 amino acids long and has a bipartite polarity profile characteristic of presequences involved in targeting to the intermembrane space of fungal mitochondria. It consists of a positively charged NH2-terminal part which resembles “matrix targeting domains” and an adjacent hydrophobic region showing sequence similarities to “intramitochondrial sorting domains”. The amino-terminal region of potato cytochrome c 1 is the first presequence of a plant protein of the mitochondrial intermembrane space to be determined and may be useful in the study of intramitochondrial sorting in plants.
    Type of Medium: Electronic Resource
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