ArticleJournal of molecular biology2015
The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 80 citations in OpenAlex.
- Characterization of missense variants in the signal peptide of C1 esterase inhibitor.The Journal of allergy and clinical immunology · 2026Article
- The Sec11 C-terminal short helix promotes productive engagement of internal signal sequences with the signal peptidase complex.The Journal of biological chemistry · 2026Article
- Human SRP Subunits Coordinate Protein Targeting and mRNA Quality Control.bioRxiv : the preprint server for biology · 2026Article
- Endoplasmic reticulum engagement of transcripts triggers VSG mRNA balancing in trypanosomes.PLoS pathogens · 2026Article
- A delayed translocation into the endoplasmic reticulum controls the post-translational modifications of PD-L1.Nature communications · 2026Article
- Enhanced secretion of an Agrocybe aegerita peroxygenase variant in K. phaffii using the native signal peptide.AMB Express · 2026Article
- Article
- Signal recognition particle-dependent secretome in humans.Scientific reports · 2026Article
- Mechanism of antithrombin deficiency due to the novel variant C32W in the C-terminus of the signal peptide.International journal of hematology · 2025Article
- The aggregation tendencies of the signal peptide regions of prone and not prone to aggregate proteins.Biochemistry and biophysics reports · 2025Article
- Characterization of the interaction between the Sec61 translocon complex and ppαF using optical tweezers.Protein science : a publication of the Protein Society · 2024Article
- Article
- Initiation of a ZAKα-dependent ribotoxic stress response by the innate immunity endoribonuclease RNase L.Cell reports · 2024Article
- Loss of Preproinsulin Interaction with Signal Recognition Particle Activates Protein Quality Control, Decreasing mRNA Stability.Journal of molecular biology · 2024Article
- Pathogenic signal peptide variants in the human genome.NAR genomics and bioinformatics · 2023Article
- Amyloid Precursor Protein and Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.Science advances · 2023Article
- Aberrant protein targeting activates quality control on the ribosome.Frontiers in cell and developmental biology · 2023Article
- Heat shock protein Hspa13 regulates endoplasmic reticulum and cytosolic proteostasis through modulation of protein translocation.The Journal of biological chemistry · 2022Article
- Defective Human SRP Induces Protein Quality Control and Triggers Stress Response.Journal of molecular biology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The signal recognition particle (SRP) cotranslationally recognizes signal sequences of secretory proteins and targets ribosome-nascent chain complexes to the SRP receptor in the endoplasmic reticulum membrane, initiating translocation of the nascent chain through the Sec61 translocon. Although signal sequences do not have homology, they have similar structural regions: a positively charged N-terminus, a hydrophobic core and a more polar C-terminal region that contains the cleavage site for the signal peptidase. Here, we have used site-specific photocrosslinking to study SRP-signal sequence interactions. A photoreactive probe was incorporated into the middle of wild-type or mutated signal sequences of the secretory protein preprolactin by in vitro translation of mRNAs containing an amber-stop codon in the signal peptide in the presence of the N(ε)-(5-azido-2 nitrobenzoyl)-Lys-tRNA(amb) amber suppressor. A homogeneous population of SRP-ribosome-nascent chain complexes was obtained by the use of truncated mRNAs in translations performed in the presence of purified canine SRP. Quantitative analysis of the photoadducts revealed that charged residues at the N-terminus of the signal sequence or in the early part of the mature protein have only a mild effect on the SRP-signal sequence association. However, deletions of amino acid residues in the hydrophobic portion of the signal sequence severely affect SRP binding. The photocrosslinking data correlate with targeting efficiency and translocation across the membrane. Thus, the hydrophobic core of the signal sequence is primarily responsible for its recognition and binding by SRP, while positive charges fine-tune the SRP-signal sequence affinity and targeting to the translocon.
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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.