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 complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins.

The EMBO journal - 15 Nov 1995

Hauser S, Bacher G, Dobberstein B, Lütcke H

Abstract excerpt

Translocation of proteins across the endoplasmic reticulum membrane is initiated by the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex consisting of a 7S RNA and six polypeptides. To investigate the functions of the SRP components, we have tested the activities of several SRP subparticles. We show that the SRP GTPase (SRP54) alone binds a signal sequence and discriminates it from a...

Read the complete abstract on PubMed

Topics

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

Share to Biological Transport
Share to Cytosol
Share to Guanosine Triphosphate

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

Share to Intracellular Membranes

Share to Mutation

Share to Protein Binding

Share to Protein Sorting Signals

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 8521805
DOI: 10.1002/j.1460-2075.1995.tb00235.x
PMCID: PMC394662

Genes

SRP54

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

A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins.PMID 8521805Read ↗

Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP.Semantic proximity Read ↗

The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting.Semantic proximity Read ↗

Molecular evolution of SRP cycle components: functional implications.Semantic proximity Read ↗

Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Semantic proximity Read ↗

Roles for Srp72p in assembly, nuclear export and function of the signal recognition particle.Semantic proximity Read ↗

Genetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p.Semantic proximity Read ↗

Elongation arrest is a physiologically important function of signal recognition particle.Semantic proximity Read ↗

Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation.Semantic proximity Read ↗

SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.Semantic proximity Read ↗

Binding site of the M-domain of human protein SRP54 determined by systematic site-directed mutagenesis of signal recognition particle RNA.Semantic proximity Read ↗

The signal recognition particle in S. cerevisiae.Semantic proximity Read ↗

Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica.Semantic proximity Read ↗

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