Activities of Escherichia coli ribosomes in IF3 and RMF change to prepare 100S ribosome formation on entering the stationary growth phase
- PMID: 19170772
- DOI: 10.1111/j.1365-2443.2008.01272.x
Activities of Escherichia coli ribosomes in IF3 and RMF change to prepare 100S ribosome formation on entering the stationary growth phase
Abstract
The canonical ribosome cycle in bacteria consists of initiation, elongation, termination, and recycling stages. After the recycling stage, initiation factor 3 (IF3) stabilizes ribosomal dissociation by binding to 30S subunits for the next round of translation. On the other hand, during the stationary growth phase, it has been elucidated that Escherichia coli ribosomes are dimerized (100S ribosome formation) by binding ribosome modulation factor (RMF) and hibernation promoting factor (HPF), leading to a hibernation stage. This indicates that 100S ribosomes are formed after these factors are scrambled for ribosomes concomitantly with transition from the log phase to the stationary phase. In this study, to elucidate the ribosomal events before 100S ribosome formation, the relationships between protein factors (RMF and HPF) involved in 100S ribosome formation and IF3 involved in initiation complex formation were examined. As a result of in vitro assays, it was found that ribosomal dissociation activity by IF3 fell, and that ribosomal dimerization activity by RMF and HPF was elevated more when using stationary-phase ribosomes than when using log-phase ribosomes. This suggests that ribosomes change into forms which are hard to bind with IF3 and easy to form 100S ribosomes by RMF and HPF concomitantly with transition from the log phase to the stationary phase.
Similar articles
-
Role of HPF (hibernation promoting factor) in translational activity in Escherichia coli.J Biochem. 2008 Mar;143(3):425-33. doi: 10.1093/jb/mvm243. Epub 2008 Jan 2. J Biochem. 2008. PMID: 18174192
-
Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli.Genes Cells. 2005 Dec;10(12):1103-12. doi: 10.1111/j.1365-2443.2005.00903.x. Genes Cells. 2005. PMID: 16324148
-
Ribosome modulation factor: stationary growth phase-specific inhibitor of ribosome functions from Escherichia coli.Biochem Biophys Res Commun. 1995 Sep 14;214(2):410-7. doi: 10.1006/bbrc.1995.2302. Biochem Biophys Res Commun. 1995. PMID: 7677746
-
[Structure and function of 100S ribosome found in the stationary growth phase of Escherichia coli].Tanpakushitsu Kakusan Koso. 2006 Jul;51(8):966-71. Tanpakushitsu Kakusan Koso. 2006. PMID: 16838671 Review. Japanese. No abstract available.
-
Growth phase coupled modulation of Escherichia coli ribosomes.Genes Cells. 1998 Apr;3(4):203-8. doi: 10.1046/j.1365-2443.1998.00187.x. Genes Cells. 1998. PMID: 9663655 Review.
Cited by
-
K63 polyubiquitination is a new modulator of the oxidative stress response.Nat Struct Mol Biol. 2015 Feb;22(2):116-23. doi: 10.1038/nsmb.2955. Epub 2015 Jan 26. Nat Struct Mol Biol. 2015. PMID: 25622294 Free PMC article.
-
Characterization of hibernating ribosomes in mammalian cells.Cell Cycle. 2011 Aug 15;10(16):2691-702. doi: 10.4161/cc.10.16.16844. Epub 2011 Aug 15. Cell Cycle. 2011. PMID: 21768774 Free PMC article.
-
Ribosomal Hibernation-Associated Factors in Escherichia coli.Microorganisms. 2021 Dec 24;10(1):33. doi: 10.3390/microorganisms10010033. Microorganisms. 2021. PMID: 35056482 Free PMC article. Review.
-
Heterogeneous rpoS and rhlR mRNA levels and 16S rRNA/rDNA (rRNA gene) ratios within Pseudomonas aeruginosa biofilms, sampled by laser capture microdissection.J Bacteriol. 2010 Jun;192(12):2991-3000. doi: 10.1128/JB.01598-09. Epub 2010 Mar 26. J Bacteriol. 2010. PMID: 20348255 Free PMC article.
-
Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ.J Cell Biol. 2010 Aug 23;190(4):613-21. doi: 10.1083/jcb.201005007. J Cell Biol. 2010. PMID: 20733057 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials