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Article

Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import.

The EMBO journal - 1 May 1996

Hönlinger A, Bömer U, Alconada A, Eckerskorn C, Lottspeich F, Dietmeier K, Pfanner N

Abstract excerpt

The preprotein translocase of the outer mitochondrial membrane is a multi-subunit complex with receptors and a general import pore. We report the molecular identification of Tom7, a small subunit of the translocase that behaves as an integral membrane protein. The deletion of TOM7 inhibited the mitochondrial import of the outer membrane protein porin, whereas the import of preproteins destined for the...

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Identifiers

PMID: 8641278
PMCID: PMC450135

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import.PMID 8641278Read ↗

Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex.Semantic proximity Read ↗

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Coupling of mitochondrial import and export translocases by receptor-mediated supercomplex formation.Semantic proximity Read ↗

Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10.Semantic proximity Read ↗

Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria.Semantic proximity Read ↗

Biogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Semantic proximity Read ↗

Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.Semantic proximity Read ↗

Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa.Semantic proximity Read ↗

Biogenesis of Tim23 and Tim17, integral components of the TIM machinery for matrix‐targeted preproteinsSemantic proximity Read ↗

The channel-forming Sym1 protein is transported by the TIM23 complex in a presequence-independent manner.Semantic proximity Read ↗

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