Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.

Nature structural & molecular biology - 1 Nov 2004

D'Silva Patrick, Liu Qinglian, Walter William, Craig Elizabeth A

Abstract excerpt

Preproteins synthesized on cytosolic ribosomes, but destined for the mitochondrial matrix, pass through the presequence translocase of the inner membrane. Translocation is driven by the import motor, having at its core the essential chaperone mtHsp70 (Ssc1 in yeast). MtHsp70 is tethered to the translocon channel at the matrix side of the inner membrane by the peripheral membrane protein Tim44. A key question in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anisotropy
Share to HSP70 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Immunoprecipitation

Share to Intracellular Membranes

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 15489862
DOI: 10.1038/nsmb846

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.PMID 15489862Read ↗

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 ↗

Mitochondrial Hsp70/MIM44 complex facilitates protein import.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 ↗

Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44.Semantic proximity Read ↗

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

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

Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.Semantic proximity Read ↗

The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Semantic proximity Read ↗

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

Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space.Semantic proximity Read ↗

Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins.Semantic proximity Read ↗

An intramembrane chaperone complex facilitates membrane protein biogenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.