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

Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.

The Journal of biological chemistry - 23 Feb 2018

Mori Hiroyuki, Sakashita Sohei, Ito Jun, Ishii Eiji, Akiyama Yoshinori

Abstract excerpt

VemP ( Vibrio protein export monitoring polypeptide) is a secretory protein comprising 159 amino acid residues, which functions as a secretion monitor in Vibrio and regulates expression of the downstream V.secDF2 genes. When VemP export is compromised, its translation specifically undergoes elongation arrest at the position where the Gln156 codon of vemP encounters the P-site in the translating ribosome,...

Read the complete abstract on PubMed

Topics

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

Share to Lac Operon
Share to Oligopeptides
Share to Peptide Chain Termination, Translational

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Engineering

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Ribosomes

Share to Vibrio

Source

Open in PubMed Open full text

Identifiers

PMID: 29317498
DOI: 10.1074/jbc.M117.816561
PMCID: PMC5827439

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.PMID 29317498Read ↗

The ribosomal exit tunnel functions as a discriminating gate.Semantic proximity Read ↗

Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Semantic proximity Read ↗

Translation arrest requires two-way communication between a nascent polypeptide and the ribosome.Semantic proximity Read ↗

Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.Semantic proximity Read ↗

The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel.Semantic proximity Read ↗

Identification of a SecM segment required for export-coupled release from elongation arrest.Semantic proximity Read ↗

Translation arrest of SecM is essential for the basal and regulated expression of SecA.Semantic proximity Read ↗

Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Semantic proximity Read ↗

Identification of a hyperactive variant of the SecM motif involved in ribosomal arrest.Semantic proximity Read ↗

Global analysis of translation termination in E. coli.Semantic proximity Read ↗

Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons.Semantic proximity Read ↗

Exploration of the arrest peptide sequence space reveals arrest-enhanced variants.Semantic proximity Read ↗

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