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Article

Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.

The international journal of biochemistry & cell biology - 1 Nov 2009

Schiller Dirk

Abstract excerpt

Import of proteins into the matrix is driven by the Tim23 presequence translocase-associated import motor PAM. The core component of PAM is the mitochondrial chaperone mtHsp70, which ensures efficient translocation of proteins across the inner membrane through interactions with the J-protein complex Pam16-Pam18 (Tim16-Tim14) and its cochaperone Tim44. The recently identified non-essential Pam17 is a further...

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Source

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Identifiers

PMID: 19577659
DOI: 10.1016/j.biocel.2009.06.011
PMCID: PMC3353651

Genes

PAM

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.PMID 19577659Read ↗

Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane.Semantic proximity Read ↗

Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.Semantic proximity Read ↗

Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.Semantic proximity Read ↗

Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.Semantic proximity Read ↗

Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.Semantic proximity Read ↗

Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.Semantic proximity Read ↗

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

The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.Semantic proximity Read ↗

Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.Semantic proximity Read ↗

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

Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane.Semantic proximity Read ↗

Hotspots for Disease-Causing Mutations in the Mitochondrial TIM23 Import Complex.Semantic proximity Read ↗

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