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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1187 (1994), S. 270-274 
    ISSN: 0005-2728
    Keywords: Chaperone ; Cytochrome biogenesis ; Import receptor ; Mitochondrion ; Protein folding ; Protein import
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 263 (2000), S. 527-534 
    ISSN: 1617-4623
    Keywords: Key words Mitochondrial DnaJ ; Mdj1p ; Mitochondrial DNA ; Complementation ; Chaperone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Inactivation of the gene for the mitochondrial DnaJ homolog, Mdj1p, in Saccharomyces cerevisiae results in temperature sensitivity and the loss of respiratory activity; the latter phenotype has been attributed to the loss of mitochondrial DNA. To investigate the functional specificity of Mdj1p, non-mitochondrial DnaJ proteins were targeted to mitochondria and tested for their ability to substitute for Mdj1p. The tested DnaJ proteins were able to complement the two Mdj1p-linked phenotypes, i.e., respiratory activity and growth at 37 °C, to different extents, ranging from full to very poor complementation. All DnaJ homologs ensured faithful propagation of the mitochondrial genome. N-terminal fragments of Mdj1p and Escherichia coli DnaJ comprising the well-characterized J domain partially substituted for Mdj1p. As the only hitherto known function of the N-terminal fragment is modulation of the substrate binding activity of the cognate Hsp70, we conclude that both Mdj1p-linked phenotypes – maintenance of respiratory activity and the ability to grow at elevated temperature – involve a mitochondrial Hsp70 partner protein.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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