How mitochondria import hydrophilic and hydrophobic proteins

• Agnieszka Chacinska ^[1] ; Nikolaus Pfanner ^[1] ; Chris Meisinger ^[1]
  1. [1] University of Education Freiburg

     University of Education Freiburg

     Stadtkreis Freiburg im Breisgau, Alemania

     
• Localización: Trends in cell biology, ISSN 0962-8924, Vol. 12, Nº 7, 2002, págs. 299-303
• Idioma: inglés
• Texto completo no disponible (Saber más ...)
• Resumen

  • Most mitochondrial proteins are nuclear encoded and have to be transported into the organelle after synthesis on cytosolic ribosomes. Three multimeric protein complexes have been identified that import precursor proteins destined for the mitochondria: the TOM complex in the outer membrane and two TIM complexes in the inner membrane. Recent work has provided a detailed view of the different mechanisms operating during the import of the two major classes of mitochondrial proteins – hydrophilic proteins with cleavable presequences and hydrophobic proteins with multiple internal signals.