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

FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon.

EMBO reports - 1 May 2005

Angelini Sandra, Deitermann Sandra, Koch Hans-Georg

Abstract excerpt

Co-translational membrane targeting of proteins by the bacterial signal-recognition particle (SRP) requires the specific interaction of the SRP-ribosome nascent chain complex with FtsY, the bacterial SRP receptor (SR). FtsY is homologous to the SRalpha-subunit of the eukaryotic SR, which is tethered to the endoplasmic-reticulum membrane by its interaction with the integral SRbeta-subunit. In contrast to SRalpha,...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Cell Membrane
Share to Escherichia coli

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

Share to Escherichia coli Proteins

Share to Protein Structure, Tertiary

Share to Receptors, Cytoplasmic and Nuclear

Share to SEC Translocation Channels

Share to Signal Recognition Particle

Source

Open in PubMed Open full text

Identifiers

PMID: 15815684
DOI: 10.1038/sj.embor.7400385
PMCID: PMC1299298

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

FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon.PMID 15815684Read ↗

Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites.Semantic proximity Read ↗

A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.Semantic proximity Read ↗

A molecular modeling study of the interaction between SRP-receptor complex and peptide translocon.Semantic proximity Read ↗

Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY.Semantic proximity Read ↗

Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.Semantic proximity Read ↗

Structure and Switch Cycle of SRβ as Ancestral Eukaryotic GTPase Associated with Secretory Membranes.Semantic proximity Read ↗

Mechanism of association and reciprocal activation of two GTPases.Semantic proximity Read ↗

An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.Semantic proximity Read ↗

SecA mediates cotranslational targeting and translocation of an inner membrane protein.Semantic proximity Read ↗

Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Semantic proximity Read ↗

Evidence for a novel GTPase priming step in the SRP protein targeting pathway.Semantic proximity Read ↗

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.Semantic proximity Read ↗

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