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Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle
- Source :
- PloS Biology, 18(9):e3000874, 1-33. Public Library of Science, PLoS Biology, PLoS Biology, Vol 18, Iss 9, p e3000874 (2020), PLOS Biology, Steinberg, R, Origi, A, Natriashvili, A, Sarmah, P, Licheva, M, Walker, P M, Kraft, C, High, S, Luirink, J, Shi, W Q, Helmstädter, M, Ulbrich, M H & Koch, H G 2020, ' Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle ', PloS Biology, vol. 18, no. 9, e3000874, pp. 1-33 . https://doi.org/10.1371/journal.pbio.3000874
- Publication Year :
- 2020
-
Abstract
- Small membrane proteins represent a largely unexplored yet abundant class of proteins in pro- and eukaryotes. They essentially consist of a single transmembrane domain and are associated with stress response mechanisms in bacteria. How these proteins are inserted into the bacterial membrane is unknown. Our study revealed that in Escherichia coli, the 27-amino-acid-long model protein YohP is recognized by the signal recognition particle (SRP), as indicated by in vivo and in vitro site-directed cross-linking. Cross-links to SRP were also observed for a second small membrane protein, the 33-amino-acid-long YkgR. However, in contrast to the canonical cotranslational recognition by SRP, SRP was found to bind to YohP posttranslationally. In vitro protein transport assays in the presence of a SecY inhibitor and proteoliposome studies demonstrated that SRP and its receptor FtsY are essential for the posttranslational membrane insertion of YohP by either the SecYEG translocon or by the YidC insertase. Furthermore, our data showed that the yohP mRNA localized preferentially and translation-independently to the bacterial membrane in vivo. In summary, our data revealed that YohP engages an unique SRP-dependent posttranslational insertion pathway that is likely preceded by an mRNA targeting step. This further highlights the enormous plasticity of bacterial protein transport machineries.<br />Small membrane proteins represent a largely unexplored yet abundant class of proteins, but how they are inserted into the bacterial membrane is unknown. This study identifies a novel posttranslational protein transport pathway that relies on the signal recognition particle and the SecYEG translocon/YidC insertase.
- Subjects :
- 0301 basic medicine
Cell Membranes
Plasma protein binding
Protein Synthesis
Biochemistry
Physical Chemistry
environment and public health
0302 clinical medicine
Protein biosynthesis
Cross-Linking
Biology (General)
Integral membrane protein
Signal recognition particle
General Neuroscience
Messenger RNA
Escherichia coli Proteins
Chemical Synthesis
Cell biology
Transport protein
Nucleic acids
Transmembrane domain
Chemistry
Protein Transport
Physical Sciences
Cellular Structures and Organelles
General Agricultural and Biological Sciences
Research Article
Surface Chemistry
Protein Binding
Biosynthetic Techniques
QH301-705.5
Biology
Research and Analysis Methods
Models, Biological
General Biochemistry, Genetics and Molecular Biology
03 medical and health sciences
Escherichia coli
Integral Membrane Proteins
Amino Acid Sequence
RNA, Messenger
SecYEG Translocon
General Immunology and Microbiology
Chemical Bonding
Biology and Life Sciences
Membrane Proteins
Proteins
Cell Biology
Outer Membrane Proteins
030104 developmental biology
Membrane protein
Protein Biosynthesis
Artificial Membranes
RNA
Ribosomes
Protein Processing, Post-Translational
Signal Recognition Particle
030217 neurology & neurosurgery
SEC Translocation Channels
Subjects
Details
- Language :
- English
- ISSN :
- 15449173
- Database :
- OpenAIRE
- Journal :
- PloS Biology, 18(9):e3000874, 1-33. Public Library of Science, PLoS Biology, PLoS Biology, Vol 18, Iss 9, p e3000874 (2020), PLOS Biology, Steinberg, R, Origi, A, Natriashvili, A, Sarmah, P, Licheva, M, Walker, P M, Kraft, C, High, S, Luirink, J, Shi, W Q, Helmstädter, M, Ulbrich, M H & Koch, H G 2020, ' Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle ', PloS Biology, vol. 18, no. 9, e3000874, pp. 1-33 . https://doi.org/10.1371/journal.pbio.3000874
- Accession number :
- edsair.doi.dedup.....1c8e9c6eb366c38d98ed63a9527c1bba