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Stress response as implemented by hibernating ribosomes: a structural overview
- Source :
- The Febs Journal
- Publication Year :
- 2019
- Publisher :
- Wiley, 2019.
-
Abstract
- Protein synthesis is one of the most energy demanding cellular processes. The ability to regulate protein synthesis is essential for cells under normal as well as stress conditions, such as nutrient deficiencies. One mechanism for protein synthesis suppression is the dimerization of ribosomes into hibernation complexes. In most cells, this process is promoted by the hibernating promoting factor (HPF) and in a small group of Gram-negative bacteria (γ-proteobacteria), the dimer formation is induced by a shorter version of HPF (HPFshort ) and by an additional protein, the ribosome modulation factor. In most bacteria, the product of this process is the 100S ribosome complex. Recent advances in cryogenic electron microscopy methods resulted in an abundance of detailed structures of near atomic resolutions 100S complexes that allow for a better understanding of the dimerization process and the way it inhibits protein synthesis. As ribosomal dimerization is vital for cell survival, this process is an attractive target for the development of novel antimicrobial substances that might inhibit or stabilize the complex formation. As different dimerization processes exist among bacteria, including pathogens, this process may provide the basis for species-specific design of antimicrobial agents. Here, we review in detail the various dimerization mechanisms and discuss how they affect the overall dimer structures of the bacterial ribosomes.
- Subjects :
- Ribosomal Proteins
0301 basic medicine
Cell Survival
Protein Conformation
Dimer
Biochemistry
Ribosome
Fight-or-flight response
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Hibernation
Protein biosynthesis
Structural Snapshot
single particle cryo‐EM
Molecular Biology
100S
biology
Chemistry
Mechanism (biology)
Escherichia coli Proteins
Cryoelectron Microscopy
Cell Biology
Ribosomal RNA
biology.organism_classification
Modulation factor
030104 developmental biology
ribosome
Protein Biosynthesis
030220 oncology & carcinogenesis
Biophysics
Energy Metabolism
Dimerization
Ribosomes
Gammaproteobacteria
Bacteria
Protein Binding
Subjects
Details
- ISSN :
- 17424658 and 1742464X
- Volume :
- 286
- Database :
- OpenAIRE
- Journal :
- The FEBS Journal
- Accession number :
- edsair.doi.dedup.....f32d608eb0e2ed17efbb75a7cc2c17e5