Burakovsky, Dmitry E.

[["dc.bibliographiccitation.firstpage","1848"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1853"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Burakovsky, Dmitry E."],["dc.contributor.author","Sergiev, Petr V."],["dc.contributor.author","Steblyanko, Maria A."],["dc.contributor.author","Kubarenko, Andriy V."],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Bogdanov, Alexey A."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Dontsova, Olga A."],["dc.date.accessioned","2017-09-07T11:45:20Z"],["dc.date.available","2017-09-07T11:45:20Z"],["dc.date.issued","2010"],["dc.description.abstract","During protein synthesis, aminoacyl-tRNA (aa-tRNA) and release factors 1 and 2 (RF1 and RF2) have to bind at the catalytic center of the ribosome on the 50S subunit where they take part in peptide bond formation or peptidyl-tRNA hydrolysis, respectively. Computer simulations of aa-tRNA movement into the catalytic site (accommodation) suggested that three nucleotides of 23S rRNA, U2492, C2556, and C2573, form a \"gate\" at which aa-tRNA movement into the A site is retarded. Here we examined the role of nucleotides C2573 of 23S rRNA, a part of the putative accommodation gate, and of the neighboring A2572 for aa-tRNA binding followed by peptide bond formation and for the RF2-dependent peptide release. Mutations at the two positions did not affect aa-tRNA accommodation, peptide bond formation, or the fidelity of aa-tRNA selection, but impaired RF2-catalyzed peptide release. The data suggest that the ribosome is a robust machine that allows rapid aa-tRNA accommodation despite the defects at the accommodation gate. In comparison, peptide release by RF2 appears more sensitive to these mutations, due to slower accommodation of the factor or effects on RF2 positioning in the A site."],["dc.identifier.doi","10.1261/rna.2185710"],["dc.identifier.gro","3142870"],["dc.identifier.isi","000281003900013"],["dc.identifier.pmid","20668033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/321"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1355-8382"],["dc.title","Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7885"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","7895"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Burakovsky, Dmitry E."],["dc.contributor.author","Prokhorova, Irina V."],["dc.contributor.author","Sergiev, Petr V."],["dc.contributor.author","Milón, Pohl"],["dc.contributor.author","Sergeeva, Olga V."],["dc.contributor.author","Bogdanov, Alexey A."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Dontsova, Olga A."],["dc.date.accessioned","2018-01-29T11:43:19Z"],["dc.date.available","2018-01-29T11:43:19Z"],["dc.date.issued","2012"],["dc.description.abstract","The functional centers of the ribosome in all organisms contain ribosomal RNA (rRNA) modifications, which are introduced by specialized enzymes and come at an energy cost for the cell. Surprisingly, none of the modifications tested so far was essential for growth and hence the functional role of modifications is largely unknown. Here, we show that the methyl groups of nucleosides m(2)G966 and m(5)C967 of 16S rRNA in Escherichia coli are important for bacterial fitness. In vitro analysis of all phases of translation suggests that the m(2)G966/m(5)C967 modifications are dispensable for elongation, termination and ribosome recycling. Rather, the modifications modulate the early stages of initiation by stabilizing the binding of fMet-tRNA(fMet) to the 30S pre-initiation complex prior to start-codon recognition. We propose that the m(2)G966 and m(5)C967 modifications help shaping the bacterial proteome, most likely by fine-tuning the rates that determine the fate of a given messenger RNA (mRNA) at early checkpoints of mRNA selection."],["dc.identifier.doi","10.1093/nar/gks508"],["dc.identifier.pmid","22649054"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11875"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1362-4962"],["dc.title","Impact of methylations of m2G966/m5C967 in 16S rRNA on bacterial fitness and translation initiation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]