ArticleProceedings of the National Academy of Sciences of the United States of America2009
Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 80 citations in OpenAlex.
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- Deciphering the Interdomain Coupling in a Gram-Negative Bacterial Membrane Insertase.The journal of physical chemistry. B · 2024Article
- Signal recognition particle RNA is critical for genetic competence and virulence ofJournal of bacteriology · 2024Article
- NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes.International journal of molecular sciences · 2023Article
- Cardiolipin occupancy profiles of YidC paralogs reveal the significance of respective TM2 helix residues in determining paralog-specific phenotypes.Frontiers in molecular biosciences · 2023Article
- An investigation of the YidC-mediated membrane insertion of Pf3 coat protein using molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- Article
- The Role of a Crystallographically Unresolved Cytoplasmic Loop in Stabilizing the Bacterial Membrane Insertase YidC2.Scientific reports · 2019Article
- Membrane proteomic analysis reveals overlapping and independent functions of Streptococcus mutans Ffh, YidC1, and YidC2.Molecular oral microbiology · 2019Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Comprehensive subcellular topologies of polypeptides in Streptomyces.Microbial cell factories · 2018Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Pseudomonas stutzeri as an alternative host for membrane proteins.Microbial cell factories · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015Review
- Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Molecular oral microbiology · 2015Review
- Hydrophilic microenvironment required for the channel-independent insertase function of YidC protein.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- MifM monitors total YidC activities of Bacillus subtilis, including that of YidC2, the target of regulation.Journal of bacteriology · 2015Article
- Streptococcus mutans extracellular DNA is upregulated during growth in biofilms, actively released via membrane vesicles, and influenced by components of the protein secretion machinery.Journal of bacteriology · 2014Article
- YlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutans.Journal of bacteriology · 2014Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
YidC/Oxa/Alb3 family proteins catalyze the insertion of integral membrane proteins in bacteria, mitochondria, and chloroplasts, respectively. Unlike gram-negative organisms, gram-positive bacteria express 2 paralogs of this family, YidC1/SpoIIIJ and YidC2/YgjG. In Streptococcus mutans, deletion of yidC2 results in a stress-sensitive phenotype similar to that of mutants lacking the signal recognition particle (SRP) protein translocation pathway, while deletion of yidC1 has a less severe phenotype. In contrast to eukaryotes and gram-negative bacteria, SRP-deficient mutants are viable in S. mutans; however, double SRP-yidC2 mutants are severely compromised. Thus, YidC2 may enable loss of the SRP by playing an independent but overlapping role in cotranslational protein insertion into the membrane. This is reminiscent of the situation in mitochondria that lack an SRP pathway and where Oxa1 facilitates cotranslational membrane protein insertion by binding directly to translation-active ribosomes. Here, we show that OXA1 complements a lack of yidC2 in S. mutans. YidC2 also functions reciprocally in oxa1-deficient Saccharomyces cerevisiae mutants and mediates the cotranslational insertion of mitochondrial translation products into the inner membrane. YidC2, like Oxa1, contains a positively charged C-terminal extension and associates with translating ribosomes. Our results are consistent with a gene-duplication event in gram-positive bacteria that enabled the specialization of a YidC isoform that mediates cotranslational activity independent of an SRP pathway.
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