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

Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.

The Journal of biological chemistry - 5 Feb 2010

Price Claire E, Driessen Arnold J M

Abstract excerpt

All members of the Oxa1/Alb3/YidC family have been implicated in the biogenesis of respiratory and energy transducing proteins. In Escherichia coli, YidC functions together with and independently of the Sec system. Although the range of proteins shown to be dependent on YidC continues to increase, the exact role of YidC in insertion remains enigmatic. Here we show that YidC is essential for the insertion of...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Escherichia coli Proteins

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

Share to Glutamates

Share to Lysine

Share to Membrane Transport Proteins

Share to NADH Dehydrogenase

Share to Proteolipids

Share to SEC Translocation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 19959836
DOI: 10.1074/jbc.M109.051128
PMCID: PMC2823498

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

Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.PMID 19959836Read ↗

Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity.Semantic proximity Read ↗

The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential.Semantic proximity Read ↗

Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function.Semantic proximity Read ↗

Membrane protein sequence features direct post-translational insertionSemantic proximity Read ↗

Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery.Semantic proximity Read ↗

Features of membrane protein sequence direct post-translational insertion.Semantic proximity Read ↗

The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.Semantic proximity Read ↗

Functional overlap but lack of complete cross-complementation of Streptococcus mutans and Escherichia coli YidC orthologs.Semantic proximity Read ↗

Subunit a of cytochrome o oxidase requires both YidC and SecYEG for membrane insertion.Semantic proximity Read ↗

Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity.Semantic proximity Read ↗

A mutational analysis reveals new functional interactions between domains of the Oxa1 protein in Saccharomyces cerevisiae.Semantic proximity Read ↗

Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).Semantic proximity Read ↗

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