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Article

Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria.

The Journal of biological chemistry - 15 Apr 2005

Schmitt Simone, Ahting Uwe, Eichacker Lutz, Granvogl Bernhard, Go Nancy E, Nargang Frank E, Neupert Walter, Nussberger Stephan

Abstract excerpt

Transport of nuclear encoded proteins into mitochondria is mediated by multisubunit translocation machineries in the outer and inner membranes of mitochondria. The TOM complex contains receptor and pore components that facilitate the recognition of preproteins and their transfer through the outer membrane. In addition, the complex contains a set of small proteins. Tom7 and Tom6 have been found in Neurospora and...

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Identifiers

PMID: 15701639
DOI: 10.1074/jbc.M413667200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria.PMID 15701639Read ↗

Targeting and assembly of mitochondrial tail-anchored protein Tom5 to the TOM complex depend on a signal distinct from that of tail-anchored proteins dispersed in the membrane.Semantic proximity Read ↗

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The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins.Semantic proximity Read ↗

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Inactivation of the Neurospora crassa mitochondrial outer membrane protein TOM70 by repeat-induced point mutation (RIP) causes defects in mitochondrial protein import and morphology.Semantic proximity Read ↗

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