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How mitochondria import hydrophilic and hydrophobic proteins
Authors:Chacinska Agnieszka  Pfanner Nikolaus  Meisinger Chris
Institution:1. Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400085, India;2. Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400094, India;1. DIISM Università di Siena, Via Roma 56, Siena 53100, Italy;2. QuestIT S.r.l., Via Leonida Cialfi, 23, Siena 53100, Italy
Abstract: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.
Keywords:
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