Translation in Prokaryotes

Rodnina, Marina V.

doi:10.1101/cshperspect.a032664

Cited by 215 publications

(258 citation statements)

References 181 publications

(276 reference statements)

Supporting

Mentioning

226

Contrasting

Order By: Relevance

“…The ancient proto‐ribosome is supposed to have driven the catalytic reactions that were necessary to polymerize the first amino acid or amino acid–like molecules. Such a proto‐ribosome definitely evolved in parallel to the genetic code, giving birth to the complex process we know today …”

Section: Rna World and Protein Synthesismentioning

confidence: 99%

“…Such a proto-ribosome definitely evolved in parallel to the genetic code, giving birth to the complex process we know today. 8 Back to the future: which came first, tRNA or mRNA?…”

Section: Rna World and Protein Synthesismentioning

confidence: 99%

“…In bacteria, this corresponds to the recruitment of fMet-tRNA fMet to the AUG start codon (or sometimes GUG or UUG), promoted by initiation factors IF1, IF2, and IF3 (for a recent review, see Ref. 8). Strikingly, tmRNA uses neither a methionine codon nor initiation factors to correctly place the reading frame and resume translation.…”

Section: Within the Internal Orfmentioning

confidence: 99%

See 2 more Smart Citations

When transfer‐messenger RNA scars reveal its ancient origins

Guyomar

Gillet

2019

Annals of the New York Academy of Sciences

View full text Add to dashboard Cite

In bacteria, trans‐translation is the primary quality control mechanism for rescuing ribosomes arrested during translation. This key process is universally conserved and plays a crucial role in the viability and virulence of all bacteria. It is performed by transfer‐messenger RNA (tmRNA) and its protein partner small protein B (SmpB). Here, we show that tmRNA is a key molecule that could have given birth to modern protein synthesis. The traces of an ancient RNA world persist in the structure of modern tmRNA, suggesting its old origins. Therefore, since it has both tRNA and mRNA functions, tmRNA could be the missing link that allowed modern genetic code to be read by the ribosome.

show abstract

Section: Rna World and Protein Synthesismentioning

confidence: 99%

“…Such a proto-ribosome definitely evolved in parallel to the genetic code, giving birth to the complex process we know today. 8 Back to the future: which came first, tRNA or mRNA?…”

Section: Rna World and Protein Synthesismentioning

confidence: 99%

Section: Within the Internal Orfmentioning

confidence: 99%

See 1 more Smart Citation

When transfer‐messenger RNA scars reveal its ancient origins

Guyomar

Gillet

2019

Annals of the New York Academy of Sciences

View full text Add to dashboard Cite

show abstract

“…The control of protein levels in bacteria is believed to occur predominately via transcription control, "control by dilution" 33 34 . Similar to transcription control, translation can also be controlled by a dynamic pool of translational factors, such as initiation, elongation and ribosome components 35 . The processes targeted by these systems require a rapid change in the number of proteins in the cell that cannot wait for a change in RNA levels or a dilution effect.…”

Section: Translation Control Drives Changes In Cell Status and Sourcementioning

confidence: 99%

Integration of absolute multi-omics reveals translational and metabolic interplay in mixed-kingdom microbiomes

Delogu

Kunath

Arntzen

et al. 2019

Preprint

View full text Add to dashboard Cite

Microbiology is founded on well-known model organisms. For example, the majority of our fundamental knowledge regarding the quantitative levels of DNA, RNA, and protein backdates to keystone pure culture-based studies. Nowadays, meta-omic approaches allow us to directly access the molecules that constitute microbes and microbial communities, however due to a lack of absolute measurements, many original culture-derived "microbiology statutes" have not been updated or adapted to more complex microbiome settings. Within a cellulose-degrading and methanogenic consortium, we temporally measured genome-centric absolute RNA and protein levels per gene, and obtained a protein-to-RNA ratio of 10 2 -10 4 for bacterial populations, whereas Archaeal RNA/protein dynamics (10 3 -10 5 : Methanothermobacter thermoautotrophicus) were more comparable to Eukaryotic representatives humans and yeast. The linearity between transcriptome and proteome had a populationspecific change over time, highlighting a minimal subset of four functional carriers (cellulose degrader, fermenter, syntrophic acetate-oxidizer and methanogen) that coordinated their respective metabolisms, cumulating in the overarching community phenotype of converting polysaccharides to methane. Our findings show that upgrading multi-omic toolkits with traditional absolute measurements unlocks the scaling of core biological questions to dynamic and complex microbiomes, creating a deeper insight into inter-organismal relationships that drive the greater community function. 31We combined both a RNA-spike-in for MT 10,11 and the total protein approach for MP 12 for the absolute quantification of high-throughput data. We not only demonstrate that temporal SEM1b samples were comparable within the same omic layer, but also between the MT and MP. Indeed, the protein-to-RNA ratio per sample of the bacterial populations matched previous calculations for the existing example sterilized with 0.2µm sterile filters and 15 minutes boiling. Soluble sugars were identified and quantified by high-performance anion exchange chromatography (HPAEC) with pulsed amperiometric detection (PAD). For quantification, peaks were compared to linear standard curves generated with

show abstract

“…Translation is a highly dynamic process, with four major phases: initiation, elongation, termination and ribosome recycling. During each phase, ribosomes form transient complexes with auxiliary translation factors that facilitate protein synthesis 2 .…”

Section: Introductionmentioning

confidence: 99%

Translational accuracy of a tethered ribosome

Fabret

Namy

2020

Preprint

View full text Add to dashboard Cite

Ribosomes are evolutionary conserved ribonucleoprotein complexes that function as two separate subunits in all kingdoms. During translation initiation, the two subunits assemble to form the mature ribosome, which is responsible for translating the messenger RNA. When the ribosome reaches a stop codon, release factors promote translation termination and peptide release, and recycling factors then dissociate the two subunits, ready for use in a new round of translation. A tethered ribosome, called Ribo-T, in which the two subunits are covalently linked to form a single entity, was recently described in Escherichia coli 1 . A hybrid ribosomal RNA (rRNA) consisting of both the small and large subunit rRNA sequences was engineered. The ribosome with inseparable subunits generated in this way was shown to be functional and to sustain cell growth. Here, we investigated the translational properties of Ribo-T. We analyzed its behavior in -1 or +1 frameshifting, stop codon readthrough, and internal translation initiation.Our data indicate that covalent attachment of the two subunits modifies the properties of the ribosome, altering its ability to initiate and terminate translation correctly.

show abstract

Translation in Prokaryotes

Cited by 215 publications

References 181 publications

When transfer‐messenger RNA scars reveal its ancient origins

When transfer‐messenger RNA scars reveal its ancient origins

Integration of absolute multi-omics reveals translational and metabolic interplay in mixed-kingdom microbiomes

Translational accuracy of a tethered ribosome

Contact Info

Product

Resources

About