ArticleThe Journal of biological chemistry2015
Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- How mutagenesis and laboratory conditions affect the genome of the metal-resistant bacteriumJournal of bacteriology · 2026Article
- YidC fromBiomolecules · 2023Article
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Biophysical Characterization of Membrane Proteins Embedded in Nanodiscs Using Fluorescence Correlation Spectroscopy.Membranes · 2022Review
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Subunit cooperation in the Get1/2 receptor promotes tail-anchored membrane protein insertion.The Journal of cell biology · 2021Article
- Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase.Viruses · 2021Article
- An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum.Communications biology · 2021Article
- Article
- Chloroplast Ribosomes Interact With the Insertase Alb3 in the Thylakoid Membrane.Frontiers in plant science · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- The Role of a Crystallographically Unresolved Cytoplasmic Loop in Stabilizing the Bacterial Membrane Insertase YidC2.Scientific reports · 2019Article
- Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography.The protein journal · 2019Review
- The Conserved Role of YidC in Membrane Protein Biogenesis.Microbiology spectrum · 2019Article
- The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.Scientific reports · 2018Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis.Cell reports · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the YidC/Oxa1/Alb3 protein family mediate membrane protein insertion, and this process is initiated by the assembly of YidC·ribosome nascent chain complexes at the inner leaflet of the lipid bilayer. The positively charged C terminus of Escherichia coli YidC plays a significant role in ribosome binding but is not the sole determinant because deletion does not completely abrogate ribosome binding. The positively charged cytosolic loops C1 and C2 of YidC may provide additional docking sites. We performed systematic sequential deletions within these cytosolic domains and studied their effect on the YidC insertase activity and interaction with translation-stalled (programmed) ribosome. Deletions within loop C1 strongly affected the activity of YidC in vivo but did not influence ribosome binding or substrate insertion, whereas loop C2 appeared to be involved in ribosome binding. Combining the latter deletion with the removal of the C terminus of YidC abolished YidC-mediated insertion. We propose that these two regions play an crucial role in the formation and stabilization of an active YidC·ribosome nascent chain complex, allowing for co-translational membrane insertion, whereas loop C1 may be involved in the downstream chaperone activity of YidC or in other protein-protein interactions.
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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.