ArticleThe EMBO journal1996
The signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 57 citations in OpenAlex.
- The influence of downstream structured elements within mRNA on the dynamics of intersubunit rotation in ribosomes.RNA (New York, N.Y.) · 2025Article
- The human mitochondrial mRNA structurome reveals mechanisms of gene expression.Science (New York, N.Y.) · 2024Article
- System-wide analysis of RNA and protein subcellular localization dynamics.Nature methods · 2024Article
- SARS-CoV-2 3CLpro whole human proteome cleavage prediction and enrichment/depletion analysis.Computational biology and chemistry · 2022Article
- Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation.Nature communications · 2022Article
- Ribosome as a Translocase and Helicase.Biochemistry. Biokhimiia · 2021Review
- Article
- Co-temporal Force and Fluorescence Measurements Reveal a Ribosomal Gear Shift Mechanism of Translation Regulation by Structured mRNAs.Molecular cell · 2019Article
- Co-translational mechanisms of quality control of newly synthesized polypeptides.Translation (Austin, Tex.) · 2014Review
- The effects of the codon usage and translation speed on protein folding of 3D(pol) of foot-and-mouth disease virus.Veterinary research communications · 2013Article
- Article
- Electrostatics in the ribosomal tunnel modulate chain elongation rates.Journal of molecular biology · 2008Article
- Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY.EMBO reports · 2001Article
- Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity.The EMBO journal · 2000Article
- The second-largest subunit of the mouse DNA polymerase alpha-primase complex facilitates both production and nuclear translocation of the catalytic subunit of DNA polymerase alpha.Molecular and cellular biology · 1998Article
- The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins, including the alpha subunit of the signal recognition particle receptor (SR alpha), are targeted within the cell by poorly defined mechanisms. A 140 residue N-terminal domain of SR alpha targets and anchors the polypeptide to the endoplasmic reticulum membrane by a mechanism independent of the pathway involving the signal recognition particle. To investigate the mechanism of membrane anchoring, translation pause sites on the SR alpha mRNA were used to examine the targeting of translation intermediates. A strong pause site at nucleotide 507 of the mRNA open reading frame corresponded with the shortest nascent SR alpha polypeptide able to assemble on membranes. An mRNA sequence at this pause site that resembles a class of viral -1 frameshift sequences caused translation pausing when transferred into another mRNA context. Site-directed mutagenesis of the mRNA greatly reduced translation pausing without altering the polypeptide sequence, demonstrating unambiguously a role for this mRNA sequence in translation pausing. SR alpha polypeptides synthesized from the non-pausing mRNA were impaired in co-translational membrane anchoring. Furthermore, co-translational membrane assembly of SR alpha appears to anchor polysomes translating SR alpha to membranes.
Indexed as
Identifiers
8598200PMC449929W303594016What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.