Paleskava, Alena

[["dc.bibliographiccitation.firstpage","80"],["dc.bibliographiccitation.issue","7631"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","85"],["dc.bibliographiccitation.volume","540"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Wang, Zhe"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Schröder, Gunnar F."],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2017-09-07T11:44:31Z"],["dc.date.available","2017-09-07T11:44:31Z"],["dc.date.issued","2016"],["dc.description.abstract","In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNA(Sec)) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNA(Sec) recodes a UGA stop codon next to a downstream mRNA stem-loop. Here we present the structures of six intermediates on the pathway of UGA recoding in Escherichia coli by single-particle cryo-electron microscopy. The structures explain the specificity of Sec-tRNA(Sec) binding by SelB and show large-scale rearrangements of Sec-tRNA(Sec). Upon initial binding of SelB-Sec-tRNA(Sec) to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNA(Sec) covering the sarcin-ricin loop (SRL) on the 50S subunit. Subsequent codon recognition results in a local closure of the decoding site, which moves Sec-tRNA(Sec) away from the SRL and triggers a global closure of the 30S subunit shoulder domain. As a consequence, SelB docks on the SRL, activating the GTPase of SelB. These results reveal how codon recognition triggers GTPase activation in translational GTPases."],["dc.identifier.doi","10.1038/nature20560"],["dc.identifier.gro","3141595"],["dc.identifier.isi","000388916600051"],["dc.identifier.pmid","27842381"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","The pathway to GTPase activation of elongation factor SelB on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","148"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Analytical Biochemistry"],["dc.bibliographiccitation.lastpage","150"],["dc.bibliographiccitation.volume","356"],["dc.contributor.author","Kothe, Ute"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:52:31Z"],["dc.date.available","2017-09-07T11:52:31Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1016/j.ab.2006.04.038"],["dc.identifier.gro","3143626"],["dc.identifier.isi","000240170700020"],["dc.identifier.pmid","16750812"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1161"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","0003-2697"],["dc.title","Single-step purification of specific tRNAs by hydrophobic tagging"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3014"],["dc.bibliographiccitation.firstpage","3014"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","3020"],["dc.bibliographiccitation.volume","285"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:46:09Z"],["dc.date.available","2017-09-07T11:46:09Z"],["dc.date.issued","2010"],["dc.description.abstract","SelB is a specialized translation elongation factor that delivers selenocysteyl-tRNA(Sec) (Sec-tRNA(Sec)) to the ribosome. Here we show that Sec-tRNA(Sec) binds to SelB.GTP with an extraordinary high affinity (K-d = 0.2 pM). The tight binding is driven enthalpically and involves the net formation of four ion pairs, three of which may involve the Sec residue. The dissociation of tRNA from the ternary complex SelB.GTP.Sec-tRNA(Sec) is very slow (0.3 h(-1)), and GTP hydrolysis accelerates the release of Sect-RNA(Sec) by more than a million-fold (to 240 s(-1)). The affinities of Sec-tRNA(Sec) to SelB in the GDP or apoforms, or Ser-tRNA(Sec) and tRNA(Sec) to SelB in any form, are similar (K-d = 0.5 mu M). Thermodynamic coupling in binding of Sec-tRNA(Sec) and GTP to SelB ensures at the same time the specificity of Sec-versus Ser-tRNA(Sec) selection and rapid release of Sec-tRNA(Sec) from SelB after GTP cleavage on the ribosome. SelB provides an example for the evolution of a highly specialized protein-RNA complex toward recognition of unique set of identity elements. The mode of tRNA recognition by SelB is reminiscent of another specialized factor, eIF2, rather than of EF-Tu, the common delivery factor for all other aminoacyl-tRNAs, in line with a common evolutionary ancestry of SelB and eIF2."],["dc.identifier.doi","10.1074/jbc.M109.081380"],["dc.identifier.gro","3142977"],["dc.identifier.isi","000273829000016"],["dc.identifier.pmid","19940162"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/440"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9258"],["dc.title","Thermodynamic and Kinetic Framework of Selenocysteyl-tRNA(Sec) Recognition by Elongation Factor SelB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1061"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.lastpage","1067"],["dc.bibliographiccitation.volume","388"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Gromadski, Kirill B."],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","In bacteria, UGA stop codons can be recoded to direct the incorporation of selenocysteine into proteins on the ribosome. Recoding requires a selenocysteine incorporation sequence (SECIS) downstream of the UGA codon, a specialized translation factor SelB, and the non-canonical Sec-tRNA(Sec), which is formed from Ser-tRNA(Sec) by selenocysteine synthase, SelA, using selenophosphate as selenium donor. Here we describe a rapid-kinetics approach to study the mechanism of selenocysteine insertion into proteins on the ribosome. Labeling of SelB, Sec-tRNA(Sec) and other components of the translational machinery allows direct observation of the formation or dissociation of complexes by monitoring changes in the fluorescence of single dyes or fluorescence resonance energy transfer between two fluorophores. Furthermore, the structure of SelA was studied by electron cryomicroscopy (cryo-EM). We report that intact SelA from the thermophilic bacterium Moorella thermoacetica (mthSelA) can be vitrified for cryo-EM using a controlled-environment vitrification system. Two-dimensional image analysis of vitrified mthSelA images shows that SelA can adopt the wide range of orientations required for high-resolution structure determination by cryo-EM. The results indicate that mthSelA forms a homodecamer that has a ring-like structure with five bilobed wings, similar to the structure of the E coli complex determined previously."],["dc.identifier.doi","10.1515/BC.2007.108"],["dc.identifier.gro","3143426"],["dc.identifier.isi","000249947900010"],["dc.identifier.pmid","17937620"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/939"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Walter De Gruyter & Co"],["dc.relation.issn","1431-6730"],["dc.title","Towards understanding selenocysteine incorporation into bacterial proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","27906"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","27912"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T11:11:32Z"],["dc.date.available","2018-01-29T11:11:32Z"],["dc.date.issued","2012"],["dc.description.abstract","SelB is a specialized translation factor that binds GTP and GDP and delivers selenocysteyl-tRNA (Sec-tRNA(Sec)) to the ribosome. By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and release of Sec-tRNA(Sec) to the ribosome by the structural switch between GTP- and GDP-bound conformations. However, crystal structures of SelB suggested a similar domain arrangement in the apo form and GDP- and GTP-bound forms of the factor, raising the question of how SelB can fulfill its delivery function. Here, we studied the thermodynamics of guanine nucleotide binding to SelB by isothermal titration calorimetry in the temperature range between 10 and 25 °C using GTP, GDP, and two nonhydrolyzable GTP analogs, guanosine 5'-O-(γ-thio)triphosphate (GTPγS) and guanosine 5'-(β,γ-imido)-triphosphate (GDPNP). The binding of SelB to either guanine nucleotide is characterized by a large heat capacity change (-621, -467, -235, and -275 cal × mol(-1) × K(-1), with GTP, GTPγS, GDPNP, and GDP, respectively), associated with compensatory changes in binding entropy and enthalpy. Changes in heat capacity indicate a large decrease of the solvent-accessible surface area in SelB, amounting to 43 or 32 amino acids buried upon binding of GTP or GTPγS, respectively, and 15-19 amino acids upon binding GDP or GDPNP. The similarity of the GTP and GDP forms in the crystal structures can be attributed to the use of GDPNP, which appears to induce a structure of SelB that is more similar to the GDP than to the GTP-bound form."],["dc.identifier.doi","10.1074/jbc.M112.366120"],["dc.identifier.pmid","22740700"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11870"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.title","Thermodynamics of the GTP-GDP-operated conformational switch of selenocysteine-specific translation factor SelB"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]