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

Interaction between the human mitochondrial import receptors Tom20 and Tom70 in vitro suggests a chaperone displacement mechanism.

The Journal of biological chemistry - 16 Sept 2011

Fan Anna C Y, Kozlov Guennadi, Hoegl Annabelle, Marcellus Richard C, Wong Michael J H, Gehring Kalle, Young Jason C

Abstract excerpt

The mitochondrial import receptor Tom70 contains a tetratricopeptide repeat (TPR) clamp domain, which allows the receptor to interact with the molecular chaperones, Hsc70/Hsp70 and Hsp90. Preprotein recognition by Tom70, a critical step to initiate import, is dependent on these cytosolic chaperones. Preproteins are subsequently released from the receptor for translocation across the outer membrane, yet the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Membranes

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Precursors

Share to Surface Plasmon Resonance

Source

Open in PubMed Open full text

Identifiers

PMID: 21771790
DOI: 10.1074/jbc.M111.280446
PMCID: PMC3173181

Genes

TPR

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction between the human mitochondrial import receptors Tom20 and Tom70 in vitro suggests a chaperone displacement mechanism.PMID 21771790Read ↗

Interactions of the human mitochondrial protein import receptor, hTom20, with precursor proteins in vitro reveal pleiotropic specificities and different receptor domain requirements.Semantic proximity Read ↗

The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor.Semantic proximity Read ↗

Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria.Semantic proximity Read ↗

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

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

Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrix.Semantic proximity Read ↗

Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Semantic proximity Read ↗

Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats.Semantic proximity Read ↗

Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.Semantic proximity Read ↗

The protein import receptor MOM19 of yeast mitochondria.Semantic proximity Read ↗

The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.Semantic proximity Read ↗

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