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  • 1
    Electronic Resource
    Electronic Resource
    Calcium and plant organelles (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 7 (1984), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. The role of intracellular organelles in the regulation of cytosolic Ca2+ levels and whether changes in these levels affect organelle metabolism is considered. We have assessed the biochemical properties of the Ca2+ transporting systems in mitochondrial, chloroplast and microsomal fractions. It is proposed that although all of these organelles can transport Ca2+ to varying extents it would appear that in some tissues at least mitochondria do not play a significant role in the maintenance of cytosolic Ca2+. The most important Ca2+ transporting systems are probably the ATP dependent Ca2+ extrusion across the plasma membrane and Ca2+ uptake by endoplasmic reticulum, as well as light driven Ca2+ uptake by chloroplasts. Changes in cytoplasmic [Ca2+] do appear to regulate the activity of NAD kinase in chloroplasts, the mitochondrial external NADH dehydrogenase and intra-mitochondrial glutamate dehydrogenase, all of which play a key role in plant cell metabolism. Since some of these enzymes are affected by primary stimuli such as light or hormones, it is concluded that Ca2+ may act as a second messenger mediating some of the primary responses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.1984.tb01432.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification and characterisation of cultivar-specific 22-kDa heat shock proteins from mitochondria of Pisum sativum (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 103 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Pea plants (Pisum sativum L. cv. Feltham First) exposed to a heat stress of 37°C for 6 h accumulated two low molecular weight (LMW) heat shock proteins (HSPs) of molecular mass 22 kDa. The two LMW HSPs were associated with purified mitochondria. N-terminal amino acid sequencing analysis indicates that the more basic of these proteins is a novel protein. The response of other cultivars of P. sativum to heat shock revealed that up to three 22-kDa HSPs were expressed in a cultivar-specific manner. Evidence presented suggests that the different 22-kDa HSPs arise as a result of there being multiple 22-kDa HSP genes. The expression of the most basic novel HSP was studied in the Feltham First cultivar using two dimensional SDS-PAGE. Treatment of intact plants with chloramphenicol and cycloheximide prior to heat stress treatment indicated that the LMW HSPs were nuclear encoded and de novo synthesised. The response to heat shock was rapid with protein expression detected within 45 min and the protein remained in excess of 6 days following removal of the stress. The protein accumulated to very high levels with maximal expression being 2% of the total mitochondrial protein. The results are discussed in relation to the likely role of LMW HSPs in thermotolerance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1030310.x
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  • 3
    Electronic Resource
    Electronic Resource
    Dibutylchloromethyltin chloride, a potent inhibitor of electron transport in plant mitochondria (1980)
    Springer
    Journal of bioenergetics and biomembranes 12 (1980), S. 309-323 
    Details
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Dibutylchloromethyl tin chloride (DBCT) inhibits coupled and uncoupled respiration of mitochondria from potato tubers, cauliflower florets and etiolated mung bean hypocotyls with succinate andl-malate but not with external NADH or TMPD/ascorbate as substrates. Using potato and cauliflower mitochondria, DBCT at 200 pmole/mg of protein gives complete inhibition only in KCl-based media and at pH 6.8. DBCT has no effect on the internal pH of mung bean mitochondria, but does cause a decrease in the membrane potential. Electron transport through the alternative oxidase is not inhibited, neither is the ATP-synthase system. DBCT appears to interact with the functionally-distinct pool of ubiquinone associated with the oxidation of succinate andl-malate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00744691
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  • 4
    Electronic Resource
    Electronic Resource
    Introduction (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 365-366 
    Details
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02109998
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  • 5
    Electronic Resource
    Electronic Resource
    Structure-function relationships of the alternative oxidase of plant mitochondria: A model of the active site (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 367-377 
    Details
    ISSN: 1573-6881
    Keywords: Alternative oxidase ; sequence homology ; hydroxo-bridged di-iron center proteins ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract A major characteristic of plant mitochondria is the presence of a cyanide-insensitive alternative oxidase which catalyzes the reduction of oxygen to water. Current information on the properties of the oxidase is reviewed. Conserved amino acid motifs have been identified which suggest the presence of a hydroxo-bridged di-iron center in the active site of the alternative oxidase. On the basis of sequence comparison with other di-iron center proteins, a structural model for the active site of the alternative oxidase has been developed that has strong similarity to that of methane monoxygenase. Evidence is presented to suggest that the alternative oxidase of plant mitochondria is the newest member of the class II group of di-iron center proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02109999
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  • 6
    Electronic Resource
    Electronic Resource
    Floral expression of a gene encoding an E2-relatedubiquitin-conjugating protein from Arabidopsis thaliana (1994)
    Springer
    Plant molecular biology 26 (1994), S. 445-451 
    Details
    ISSN: 1573-5028
    Keywords: ubiquitin ; Arabidopsis ; flower ; senescense
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis thaliana gene (UBC6) encoding a homologue to ubiquitin-conjugating enzymes has been isolated which is capable of encoding a protein of 183 amino acids of ca. 21 kDa. Northern analysis indicates that the gene is expressed in flowers, seeds and, to a somewhat lesser extent, in 10-day seedlings but not in mature leaves, callus and pre-flowering plants. This pattern of expression is confirmed using transgenic Arabidopsis plants containing a UBC6 promoter-GUS gene fusion construct. These plants displey GUS activity in mature anthers prior to dehiscence, in developing embryos, sepals and the style after pollination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039553
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  • 7
    Electronic Resource
    Electronic Resource
    Characterisation of PHSP1, a cDNA encoding a mitochondrial HSP70 fromPisum sativum (1992)
    Springer
    Plant molecular biology 18 (1992), S. 23-32 
    Details
    ISSN: 1573-5028
    Keywords: HSP70 ; mitochondria ; pea ; protein translocation ; cDNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A pea cDNA clone,PHSP1, encoding a member of the HSP70 gene family has been isolated. DNA sequence analysis indicates that the protein encoded byPHSP1 is a homologue of the mitochondrial HSP70 proteins, SSP1 fromSchizosaccharomyces pombe and SSC1 fromS. cerevisiae. It contains an amino-terminal extension of 50 amino acids, rich in basic and hydroxyl amino acids, similar to other plant mitochondrial leader sequences. Western blot analysis indicates that the PHSP1 protein is associated only with mitochondria and not with any other sub-cellular organelle or cytoplasm. Further confirmation of its location within mitochondria was obtained fromin vitro protein translocation experiments into purifiedPisum sativum mitochondria. It was observed that the precursor protein was efficiently imported and that it is processed to produce a protein with anM r of the anticipated size of the mature protein. Results are discussed with respect to the structure and function of the mitochondrial HSP70 protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00018453
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  • 8
    Electronic Resource
    Electronic Resource
    Structure and Function of the Plant Alternative Oxidase: Its Putative Role in the Oxygen Defence Mechanism (1997)
    Springer
    Bioscience reports 17 (1997), S. 319-333 
    Details
    ISSN: 1573-4935
    Keywords: Plant alternative oxidase ; mitochondria ; oxidative stress ; active oxygen species
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Current understanding of the structure and function of the plant alternative oxidase is reviewed. In particular, the role of the oxidase in the protection of tissues against oxidative stress is developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1027388729586
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  • 9
    Electronic Resource
    Electronic Resource
    Schizosaccharomyces pombe mitochondria: Morphological, respiratory and protein import characteristics (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 923-933 
    Details
    ISSN: 0749-503X
    Keywords: mitochondria ; immunogold labelling ; HSP70 ; in vitro import ; respiration ; Q pool ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A technique is described for the isolation and purification of intact, respiratory-competent mitochondria from Sachizo-saccharomyces pombe. The purified mitochondria are capabel of oxidizing NADH and succinate as resporatory substrates. indicating the presence of succinate dehydorgenase and an NADH dehydrogenase located on the outer suface of the inner membrane. Mitochondria display good respiratory control with an ADP/O ratio of 〈2. Respiratory activity is linearly dependent upon the redox poise of the quinone pool, suggesting the presence of an unbranched repiratory pathway to molecular oxygen. Immunogold labelling using antisera raised against mitochodria proteins (SSPI, SSCI, and PHSPI) from three different species, namely S. pombe, Saccharomyces cerevisiane and the plant Pisum sativum respectively, has been used to investigate the presence and ultrastructure of the mitochondria isolated by this procedure. The immunocytochemistry was carried out using cells containing wild-type levels of SSPI protein and cells over-expressing the protein. These results also demonstrate the capacity of mitochondria to import increased levels of protein in vivo. In vitro import experiments using COXIV-DHFR indicate that purified S. pombe mitochondria can efficiently import this precursor, and that protein translocation is dependent upon an oxidizable substrate and a membrane potential.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320081103
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  • 10
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    Function of the alternative oxidase: is it still a scavenger? (2002)
    Cell Press
    Details
    Publication Date: 2002-11-01
    Print ISSN: 1360-1385
    Electronic ISSN: 1878-4372
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Published by Cell Press
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