Yet another job for the bacterial ribosome
| Autor: | Rosella Asti, Hans-Georg Koch, Ana Natriashivili, Clara Fehrenbach, Lara Knüpffer, Kärt Denks, Andrea Origi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0209 industrial biotechnology
02 engineering and technology Biology medicine.disease_cause Biochemistry Genetics and Molecular Biology (miscellaneous) Microbiology Applied Microbiology and Biotechnology Ribosome 020901 industrial engineering & automation Ribosomal protein Virology Protein targeting 0202 electrical engineering electronic engineering information engineering Genetics medicine protein targeting signal recognition particle Molecular Biology lcsh:QH301-705.5 SecYEG Translocon Signal recognition particle secyeg 020208 electrical & electronic engineering ul23 Cell Biology Ribosomal RNA Cell biology ribosome lcsh:Biology (General) Chaperone (protein) biology.protein Parasitology Protein folding seca |
| Zdroj: | Microbial Cell, Vol 6, Iss 11, Pp 524-526 (2019) |
| ISSN: | 2311-2638 |
| Popis: | The ribosome is a sophisticated cellular machine, composed of RNA and protein, which translates the mRNA-encoded genetic information into protein and thus acts at the center of gene expression. Still, the ribosome not only decodes the genetic information, it also coordinates many ribosome-associated processes like protein folding and targeting. The ribosomal protein uL23 is crucial for this coordination and is located at the ribosomal tunnel exit where it serves as binding platform for targeting factors, chaperones and modifying enzymes. This includes the signal recognition particle (SRP), which facilitates co-translational protein targeting in pro- and eukaryotes, the chaperone Trigger Factor and methionine aminopeptidase, which removes the start methionine in many bacterial proteins. A recent report revealed the intricate interaction of uL23 with yet another essential player in bacteria, the ATPase SecA, which is best known for its role during post-translational secretion of proteins across the bacterial SecYEG translocon. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|