A glimpse on Staphylococcus aureus translation machinery and its control

Khusainov, Iskander; Marenna, Alessandra; Cerciat, Marie; Fechter, Pierre; Hashem, Yaser; Marzi, Stefano; Romby, Pascale; Yusupova, G.; Yusupov, Marat

doi:10.1134/s002689331604004x

Cited by 5 publications

(8 citation statements)

References 93 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ribosomal protein bL9 may have been lost, due to a loose association with the ribosome 18 . The other missing proteins are known to be very flexible and, similar to the S taphylococcus aureus ribosome, lack sufficient density for modeling 20 . Two genes of L. lactis , llmg 0899 and llmg 2078 , have been annotated as encoding ribosomal protein uS15.…”

Section: Resultsmentioning

confidence: 99%

“…Although the C-terminal domain differs from RMF, HPF long may induce a similar conformational change in the head region of the 30S subunit to facilitate the formation of 100S dimers 4 , 6 . Alternatively, HPF long may directly trigger dimer formation upon binding at the interface, as has been suggested by Khusainov et al 20 . To determine the binding site of HPF long and the actual mechanism of HPF long -mediated dimerization, higher resolution structures are required 6 , 7 , 20 , which we provide in this study.…”

Section: Introductionmentioning

confidence: 82%

“…Alternatively, HPF long may directly trigger dimer formation upon binding at the interface, as has been suggested by Khusainov et al 20 . To determine the binding site of HPF long and the actual mechanism of HPF long -mediated dimerization, higher resolution structures are required 6 , 7 , 20 , which we provide in this study.…”

Section: Introductionmentioning

confidence: 82%

“…In a previous study 6 , we demonstrated that deletion of the C-terminal part of this dual-domain protein (hereafter named HPF long ) in Lactococcus lactis results in the loss of dimerization. Thus, whereas the N-terminal domain may have a similar role and binding site as YfiA and HPF short 20 , the C-terminal domain of HPF long is necessary for dimer formation. Although the C-terminal domain differs from RMF, HPF long may induce a similar conformational change in the head region of the 30S subunit to facilitate the formation of 100S dimers 4 , 6 .…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

et al. 2017

View full text Add to dashboard Cite

Bacteria downregulate their ribosomal activity through dimerization of 70S ribosomes, yielding inactive 100S complexes. In Escherichia coli, dimerization is mediated by the hibernation promotion factor (HPF) and ribosome modulation factor. Here we report the cryo-electron microscopy study on 100S ribosomes from Lactococcus lactis and a dimerization mechanism involving a single protein: HPFlong. The N-terminal domain of HPFlong binds at the same site as HPF in Escherichia coli 100S ribosomes. Contrary to ribosome modulation factor, the C-terminal domain of HPFlong binds exactly at the dimer interface. Furthermore, ribosomes from Lactococcus lactis do not undergo conformational changes in the 30S head domains upon binding of HPFlong, and the Shine–Dalgarno sequence and mRNA entrance tunnel remain accessible. Ribosome activity is blocked by HPFlong due to the inhibition of mRNA recognition by the platform binding center. Phylogenetic analysis of HPF proteins suggests that HPFlong-mediated dimerization is a widespread mechanism of ribosome hibernation in bacteria.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

et al. 2017

View full text Add to dashboard Cite

show abstract

“…In S. aureus , dimerization mediated by the longer SaHPF does not go through a 90S stage (Ueta et al , ). In addition, the stability of 100S dimers is proportional to the length of HPF (Ueta et al , ), which further emphasizes the importance of comparatively analyzing dimerization in bacteria (Khusainov et al , ).…”

Section: Introductionmentioning

confidence: 99%

Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF

et al. 2017

View full text Add to dashboard Cite

In bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of 100S ribosome dimers. Here, we present the structures of hibernating ribosomes from human pathogen Staphylococcus aureus containing a long variant of the hibernation-promoting factor (SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N-terminal domain (NTD) of SaHPF binds to the 30S subunit as observed for shorter variants of HPF in other species. The C-terminal domain (CTD) of SaHPF protrudes out of each ribosome in order to mediate dimerization. Using NMR, we characterized the interactions at the CTD-dimer interface. Secondary interactions are provided by helix 26 of the 16S ribosomal RNA. We also show that ribosomes in the 100S particle adopt both rotated and unrotated conformations. Overall, our work illustrates a specific mode of ribosome dimerization by long HPF, a finding that may help improve the selectivity of antimicrobials.

show abstract

Genomic analysis of RNA-Seq and sRNA-Seq data identifies potential regulatory sRNAs and their functional roles in Staphylococcus aureus

2019

View full text Add to dashboard Cite

A glimpse on Staphylococcus aureus translation machinery and its control

Cited by 5 publications

References 93 publications

A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

A general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopy

Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF

Genomic analysis of RNA-Seq and sRNA-Seq data identifies potential regulatory sRNAs and their functional roles in Staphylococcus aureus

Contact Info

Product

Resources

About