ArticleThe Journal of biological chemistry2012
Translation elongation regulates substrate selection by the signal recognition particle.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.Science advances · 2026Article
- Statistical Amplification of the Effects of Weak Magnetic Fields in Cellular Translation.Cells · 2023Article
- Mitochondrial mRNA localization is governed by translation kinetics and spatial transport.PLoS computational biology · 2022Article
- Article
- Compensating Complete Loss of Signal Recognition Particle During Co-translational Protein Targeting by the Translation Speed and Accuracy.Frontiers in microbiology · 2021Article
- Post-transcriptional control of mitochondrial protein composition in changing environmental conditions.Biochemical Society transactions · 2020Review
- A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.Nature communications · 2020Article
- Article
- Comprehensive in vivo identification of the c-Myc mRNA protein interactome using HyPR-MS.RNA (New York, N.Y.) · 2019Article
- Positive charge in the n-region of the signal peptide contributes to efficient post-translational translocation of small secretory preproteins.The Journal of biological chemistry · 2018Article
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- Article
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation.EMBO reports · 2016Article
- Altered Co-Translational Processing Plays a Role in Huntington's Pathogenesis-A Hypothesis.Frontiers in molecular neuroscience · 2016Article
- Article
- Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo.Nature structural & molecular biology · 2014Article
- Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Signal recognition particle-ribosome binding is sensitive to nascent chain length.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP) is a universally conserved cellular machinery responsible for delivering membrane and secretory proteins to the proper cellular destination. The precise mechanism by which fidelity is achieved by the SRP pathway within the in vivo environment is yet to be understood. Previous studies have focused on the SRP pathway in isolation. Here we describe another important factor that modulates substrate selection by the SRP pathway: the ongoing synthesis of the nascent polypeptide chain by the ribosome. A slower translation elongation rate rescues the targeting defect of substrate proteins bearing mutant, suboptimal signal sequences both in vitro and in vivo. Consistent with a kinetic origin of this effect, similar rescue of protein targeting was also observed with mutant SRP receptors or SRP RNAs that specifically compromise the kinetics of SRP-receptor interaction during protein targeting. These data are consistent with a model in which ongoing protein translation is in constant kinetic competition with the targeting of the nascent proteins by the SRP and provides an important factor to regulate the fidelity of substrate selection by the SRP.
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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.