The <scp>100S</scp> ribosome: ribosomal hibernation induced by stress

Yoshida, Hideji; Wada, Akira

doi:10.1002/wrna.1242

Cited by 79 publications

(96 citation statements)

References 57 publications

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“…Escherichia coli 100S ribosomes have been proposed to be 'hibernating' forms that function as a storage of intact ribosomes (Yoshida et al 2002;Yoshida & Wada 2014). This proposal is based on the quick dissociation of 100S into translationally active 70S ribosomes when a fresh rich medium is supplied (Wada et al 1990).…”

Section: Discussionmentioning

confidence: 99%

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Role of 100S ribosomes in bacterial decay period

2015

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Ribosomal proteins S10 and S2 were each fused with GFP to track the fates of these proteins in the stationary growth phase and the following decay period in Escherichia coli. The fused proteins localized mainly in the cytoplasm, and their amounts were proportional to the colony-forming unit. S10-GFP strains that lacked genes responsible for regulating 100S ribosomes and S2-GFP strain that was unable to form 100S both showed shortened stationary phases. This result indicates that these strains exhibit earlier death in the absence of 100S formation (S2-GFP, S10-GFPΔrmf and S10-GFPΔhpf) and breakdown (S10-GFPΔyfiA). Therefore, in addition to the mere presence of 100S, the correct timing of 100S formation and breakdown is required to maintain viability. We propose a model in which 100S acts as a tentative repository of ribosomes that are protected from degradation and provide a source of amino acids in later growth period.

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Section: Discussionmentioning

confidence: 99%

“…In E. coli, transcription of rmf is activated by (p)ppGpp (Izutsu et al 2001). RMF directs the dimerization of two 70S ribosomes to form the 100S ribosome in the following two-step reaction (see Yoshida & Wada 2014):…”

Section: Introductionmentioning

confidence: 99%

Role of 100S ribosomes in bacterial decay period

2015

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“…Short HPF proteins are generally found in bacteria that also harbor RMF and YfiA (to which B. burgdorferi does not appear have homologs) and are not able to dimerize ribosomes in vitro without the RMF protein (21,24). In comparison, long HPF-like proteins are thought to functionally replace both RMF and short HPF because of an extended C terminus and have been shown to dimerize ribosomes in vitro (22,68). The lack of association between BB0449 and ribosomes corresponds with the observation that short HPF proteins are unable to dimerize ribosomes without additional proteins (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…HPF subsequently binds to 90S ribosomes and covers the Aand P-sites on the 30S ribosomal subunit, preventing binding of initiator tRNA (19). Ultimately, RMF and HPF dimerize ribosomes, rendering them translationally inactive (12,(19)(20)(21)(22)(23)(24)(25). In contrast, YfiA binds to the 30S subunit of 70S ribosomes, overlapping the A-and P-sites, and prevents association of ribosomes …”

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confidence: 99%

Long-Term Survival of Borrelia burgdorferi Lacking the Hibernation Promotion Factor Homolog in the Unfed Tick Vector

et al. 2015

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Borrelia burgdorferi, a causative agent of Lyme borreliosis, is a zoonotic pathogen that survives in nutrient-limited environments within a tick, prior to transmission to its mammalian host. Survival under these prolonged nutrient-limited conditions is thought to be similar to survival during stationary phase, which is characterized by growth cessation and decreased protein production. Multiple ribosome-associated proteins are implicated in stationary-phase survival of Escherichia coli. These proteins include hibernation-promoting factor (HPF), which dimerizes ribosomes and prevents translation of mRNA. Bioinformatic analyses indicate that B. burgdorferi harbors an hpf homolog, the bb0449 gene. BB0449 protein secondary structure modeling also predicted HPF-like structure and function. However, BB0449 protein was not localized in the ribosome-associated protein fraction of in vitro-grown B. burgdorferi. In wild-type B. burgdorferi, bb0449 transcript and BB0449 protein levels are low during various growth phases. These results are inconsistent with patterns of synthesis of HPF-like proteins in other bacterial species. In addition, two independently derived bb0449 mutants successfully completed the mouse-tick infectious cycle, indicating that bb0449 is not required for prolonged survival in the nutrient-limited environment in the unfed tick or any other stage of infection by B. burgdorferi. We suggest either that BB0449 is associated with ribosomes under specific conditions not yet identified or that BB0449 of B. burgdorferi has a function other than ribosome conformation modulation. L yme disease, the most common tick-transmitted disease in the United States (1), is caused by infection with the spirochete Borrelia burgdorferi (2, 3). This pathogen's complex infectious cycle includes an Ixodes tick vector and multiple vertebrate hosts. The Ixodes tick vector, like all hard ticks, has three developmental stages: larva, nymph, and adult. Typically, larval ticks become infected with B. burgdorferi by feeding on an infected vertebrate host, often a small mammal. B. burgdorferi survives within the tick midgut (2) as larval ticks molt into nymphs (transstadial passage) and the nymphs wait to feed again, which can include overwintering (4, 5). Following the larval molt, infected nymphs can transmit B. burgdorferi to naive vertebrate hosts, which, in turn, serve as a reservoir of spirochetes for larval ticks. After fed nymphs molt, infected adult ticks can also transmit B. burgdorferi, but adults typically feed on larger animals upon which larvae do not feed. Moreover, little or no transovarial transmission of spirochetes occurs (6, 7). Therefore, adult ticks do not significantly contribute to the maintenance of B. burgdorferi populations (8), and neither do humans, which are incidental hosts of B. burgdorferi. Hence, the larval and nymphal tick life stages are relevant to the zoonotic life cycle of B. burgdorferi.It has been generally accepted that B. burgdorferi populations are sustained in nature by the long-term infect...

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“…In bacteria, the low nutrient-induced translationally inactive 100S ribosome (70S ribosome dimer) formation represents an excellent economic system that inhibits translation and stably maintains ribosomes in cells until environment conditions improve [4]. A similar mechanism (inactive 110S ribosome via 80S ribosome dimerization) has been detected in eukaryotic cells, although the details are unknown [5]; conversely, up-/down-regulation of the translation For 80S ribosome analysis, 10 pmol of purified ribosomes were incubated at 37°C for 10 min in 5 mM MgCl 2 , 25 mM KCl, 5 mM 2-mercaptoethanol, and 20 mM Tris-HCl (pH 7.6).…”

Section: Introductionmentioning

confidence: 99%