Use of protease sensitivity to probe the conformations of newly synthesised mutant forms of mitochondrial aspartate aminotransferase. (Articolo in rivista)

Type
Label
  • Use of protease sensitivity to probe the conformations of newly synthesised mutant forms of mitochondrial aspartate aminotransferase. (Articolo in rivista) (literal)
Anno
  • 1995-01-01T00:00:00+01:00 (literal)
Alternative label
  • Azzariti A, Giannattasio S, Doonan S, Merafina RS, Marra E, Quagliariello E. (1995)
    Use of protease sensitivity to probe the conformations of newly synthesised mutant forms of mitochondrial aspartate aminotransferase.
    in Biochemical and biophysical research communications (Print)
    (literal)
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  • Azzariti A, Giannattasio S, Doonan S, Merafina RS, Marra E, Quagliariello E. (literal)
Pagina inizio
  • 800 (literal)
Pagina fine
  • 807 (literal)
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  • 215 (literal)
Rivista
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  • 8 (literal)
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  • 3 (literal)
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  • Centro di Studio sui Mitocondri e Metabolismo Energetico-C.N.R., Bari, Italy. Univesity of East London, Dept Life Sciences, London, England Univ Bari, Dipartmento Biochimica & Biologia Molecolare, Bari, Italy (literal)
Titolo
  • Use of protease sensitivity to probe the conformations of newly synthesised mutant forms of mitochondrial aspartate aminotransferase. (literal)
Abstract
  • Sensitivity to digestion with pronase has been used to show that the precursor form of mitochondrial aspartate aminotransferase, the form lacking the N-terminal presequence, that with a deletion of the first 9 residues and mutants of the mature enzyme in which residue Cys-166 is mutated to alanine or serine, all retain unfolded conformations after synthesis in a reticulocyte lysate. In the presence of lysed mitochondria the various forms of mitochondrial aspartate aminotransferase retained their susceptibilities to pronase in a way that mirrored the efficiencies with which they are imported into intact mitochondria. The results are interpreted as showing that the presequence of mitochondrial aspartate aminotransferase is not uniquely required for interaction with cytosolic factors required to maintain the newly synthesised protein in a form competent for interacting with, and being imported into, mitochondria. (literal)
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