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

A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.

Molecular and cellular biology - 1 Jan 2007

Krayl Martin, Lim Joo Hyun, Martin Falk, Guiard Bernard, Voos Wolfgang

Abstract excerpt

The import of mitochondrial preproteins requires an electric potential across the inner membrane and the hydrolysis of ATP in the matrix. We assessed the contributions of the two energy sources to the translocation driving force responsible for movement of the polypeptide chain through the translocation channel and the unfolding of preprotein domains. The import-driving activity was directly analyzed by the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Membrane Potential, Mitochondrial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Molecular Motor Proteins

Share to Protein Folding

Share to Protein Precursors

Share to Tetrahydrofolate Dehydrogenase

Source

Open in PubMed Open full text

Identifiers

PMID: 17074805
DOI: 10.1128/MCB.01391-06
PMCID: PMC1800818

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.PMID 17074805Read ↗

Protein unfolding by the mitochondrial membrane potential.Semantic proximity Read ↗

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

Two distinct membrane potential-dependent steps drive mitochondrial matrix protein translocation.Semantic proximity Read ↗

A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins.Semantic proximity Read ↗

Mitochondria unfold precursor proteins by unraveling them from their N-termini.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 ↗

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 ↗

Reinvestigation of the requirement of cytosolic ATP for mitochondrial protein import.Semantic proximity Read ↗

Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence.Semantic proximity Read ↗

Insertion of an uncharged polypeptide into the mitochondrial inner membrane does not require a trans-bilayer electrochemical potential: effects of positive charges.Semantic proximity Read ↗

Mitochondrial Hsp70/MIM44 complex facilitates protein import.Semantic proximity Read ↗

Exploring the nature of the translocon-assisted protein insertion.Semantic proximity Read ↗

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