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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of the bifunctional mitochondrial processing peptidase (MPP)/bc 1 complex inSpinacia oleracea (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 285-292 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial processing peptidase MPP ; bc 1 complex ; protein import ; plant mitochondria ; cytochromec reductase ; protein processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The mitochondrial general processing peptidase (MPP) in plant mitochondria constitutes an integral part of the cytochromebc 1 complex of the respiratory chain. Here we present a characterization of this bifunctional complex from spinach leaf mitochondria. The purified MPP/bc 1 complex has a molecular mass of 550 kDa, which corresponds to a dimer. Increased ionic strength results in partial dissociation of the dimer as well as loss of the processing activity. Micellar concentrations of nonionic and zwitterionic detergents stimulate the activity by decreasing the temperature optimum of the processing reaction, whereas anionic detergents totally suppress the activity. MPP is a metalloendopeptidase. Interestingly, hemin, a potent regulator of mitochondrial and cytosolic biogenesis and inhibitor of proteosomal degradation, inhibits the processing activity. Measurements of the processing activity at different redox states of thebc 1 complex show that despite bifunctionality of the MPP/bc 1 complex, there is no correlation between electron transfer and protein processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110702
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Mitochondrial protein import in plants – Signals, Sorting, Targeting, Processing and Regulation (1998)
    Springer
    Plant molecular biology 38 (1998), S. 311-338 
    Details
    ISSN: 1573-5028
    Keywords: mitochondrial processing peptidase ; molecular chaperones ; plant mitochondria ; protein import ; processing peptidase ; protein processing ; protein sorting ; regulation of protein import ; signal peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mitochondrial biogenesis requires a coordinated expression of both the nuclear and the organellar genomes and specific intracellular protein trafficking, processing and assembly machinery. Most mitochondrial proteins are synthesised as precursor proteins containing an N-terminal extension which functions as a targeting signal, which is proteolytically cleaved off after import into mitochondria. We review our present knowledge on components and mechanisms involved in the mitochondrial protein import process in plants. This encompasses properties of targeting peptides, sorting of precursor proteins between mitochondria and chloroplasts, signal recognition, mechanism of translocation across the mitochondrial membranes and the role of cytosolic and organellar molecular chaperones in this process. The mitochondrial protein processing in plants is catalysed by the mitochondrial processing peptidase (MPP), which in contrast to other sources, is integrated into the bc1 complex of the respiratory chain. This is the most studied component of the plant import machinery characterised to date. What are the biochemical consequences of the integration of the MPP into an oligomeric protein complex and how are several hundred presequences of precursor proteins with no sequence similarities and no consensus for cleavage, specifically cleaved off by MPP? Finally we will address the emerging area of the control of protein import into mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006020208140
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    Paper (German National Licenses)
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