Goyal, Akanksha

[["dc.bibliographiccitation.firstpage","5210"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5222"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Korniy, Natalia"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Rodnina, Marina V"],["dc.date.accessioned","2020-12-10T18:19:35Z"],["dc.date.available","2020-12-10T18:19:35Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1093/nar/gkz202"],["dc.identifier.eissn","1362-4962"],["dc.identifier.issn","0305-1048"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16451"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75304"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Modulation of HIV-1 Gag/Gag-Pol frameshifting by tRNA abundance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1226"],["dc.bibliographiccitation.issue","17-18"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","1241"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Zinoviev, Alexandra"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Jindal, Supriya"],["dc.contributor.author","LaCava, John"],["dc.contributor.author","Komar, Anton A."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Hellen, Christopher U.T."],["dc.contributor.author","Pestova, Tatyana V."],["dc.date.accessioned","2022-03-01T11:46:54Z"],["dc.date.available","2022-03-01T11:46:54Z"],["dc.date.issued","2018"],["dc.description.abstract","GTP-binding protein 1 (GTPBP1) and GTPBP2 comprise a divergent group of translational GTPases with obscure functions, which are most closely related to eEF1A, eRF3, and Hbs1. Although recent reports implicated GTPBPs in mRNA surveillance and ribosome-associated quality control, how they perform these functions remains unknown. Here, we demonstrate that GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner. It also stimulates exosomal degradation of mRNAs in elongation complexes. The kinetics of GTPBP1-mediated elongation argues against its functioning in elongation per se but supports involvement in mRNA surveillance. Thus, GTP hydrolysis by GTPBP1 is not followed by rapid peptide bond formation, suggesting that after hydrolysis, GTPBP1 retains aa-tRNA, delaying its accommodation in the A site. In physiological settings, this would cause ribosome stalling, enabling GTPBP1 to elicit quality control programs; e.g., by recruiting the exosome. GTPBP1 can also deliver deacylated tRNA to the A site, indicating that it might function via interaction with deacylated tRNA, which accumulates during stresses. Although GTPBP2's binding to GTP was stimulated by Phe-tRNA Phe , suggesting that its function might also involve interaction with aa-tRNA, GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions."],["dc.description.abstract","GTP-binding protein 1 (GTPBP1) and GTPBP2 comprise a divergent group of translational GTPases with obscure functions, which are most closely related to eEF1A, eRF3, and Hbs1. Although recent reports implicated GTPBPs in mRNA surveillance and ribosome-associated quality control, how they perform these functions remains unknown. Here, we demonstrate that GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner. It also stimulates exosomal degradation of mRNAs in elongation complexes. The kinetics of GTPBP1-mediated elongation argues against its functioning in elongation per se but supports involvement in mRNA surveillance. Thus, GTP hydrolysis by GTPBP1 is not followed by rapid peptide bond formation, suggesting that after hydrolysis, GTPBP1 retains aa-tRNA, delaying its accommodation in the A site. In physiological settings, this would cause ribosome stalling, enabling GTPBP1 to elicit quality control programs; e.g., by recruiting the exosome. GTPBP1 can also deliver deacylated tRNA to the A site, indicating that it might function via interaction with deacylated tRNA, which accumulates during stresses. Although GTPBP2's binding to GTP was stimulated by Phe-tRNA Phe , suggesting that its function might also involve interaction with aa-tRNA, GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions."],["dc.identifier.doi","10.1101/gad.314724.118"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103840"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1549-5477"],["dc.relation.issn","0890-9369"],["dc.title","Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3113"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Cell reports"],["dc.bibliographiccitation.lastpage","3122"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Belardinelli, Riccardo"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-17T12:51:50Z"],["dc.date.available","2018-01-17T12:51:50Z"],["dc.date.issued","2017-09-26"],["dc.description.abstract","Canonical translation initiation in bacteria entails the assembly of the 30S initiation complex (IC), which binds the 50S subunit to form a 70S IC. IF3, a key initiation factor, is recruited to the 30S subunit at an early stage and is displaced from its primary binding site upon subunit joining. We employed four different FRET pairs to monitor IF3 relocation after 50S joining. IF3 moves away from the 30S subunit, IF1 and IF2, but can remain bound to the mature 70S IC. The secondary binding site is located on the 50S subunit in the vicinity of ribosomal protein L33. The interaction between IF3 and the 50S subunit is largely electrostatic with very high rates of IF3 binding and dissociation. The existence of the non-canonical binding site may help explain how IF3 participates in alternative initiation modes performed directly by the 70S ribosomes, such as initiation on leaderless mRNAs or re-initiation."],["dc.identifier.doi","10.1016/j.celrep.2017.09.012"],["dc.identifier.pmid","28954228"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11690"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","2211-1247"],["dc.title","Non-canonical Binding Site for Bacterial Initiation Factor 3 on the Large Ribosomal Subunit"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5282"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5298"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Yi, Sung-Hui"],["dc.contributor.author","Petrychenko, Valentyn"],["dc.contributor.author","Schliep, Jan Erik"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Chari, Ashwin"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina V"],["dc.contributor.author","Adio, Sarah"],["dc.contributor.author","Fischer, Niels"],["dc.date.accessioned","2022-06-01T09:39:22Z"],["dc.date.available","2022-06-01T09:39:22Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of codon recognition by kinetic methods using eIF1A as a reporter. Both approaches capture two distinct ribosome populations formed on an mRNA with a cognate AUG codon in the presence of eIF1, eIF1A, eIF2–GTP–Met-tRNAiMet and eIF3. The ‘open’ 40S subunit conformation differs from the human 48S scanning complex and represents an intermediate preceding the codon recognition step. The ‘closed’ form is similar to reported structures of complexes from yeast and mammals formed upon codon recognition, except for the orientation of eIF1A, which is unique in our structure. Kinetic experiments show how various initiation factors mediate the population distribution of open and closed conformations until 60S subunit docking. Our results provide insights into the timing and structure of human translation initiation intermediates and suggest the differences in the mechanisms of start codon selection between mammals and yeast."],["dc.identifier.doi","10.1093/nar/gkac283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108454"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","Conformational rearrangements upon start codon recognition in human 48S translation initiation complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10700"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","10712"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Belardinelli, Riccardo"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Milón, Pohl"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:54:48Z"],["dc.date.available","2017-09-07T11:54:48Z"],["dc.date.issued","2015"],["dc.description.abstract","The transition of the 30S initiation complex (IC) to the translating 70S ribosome after 50S subunit joining provides an important checkpoint for mRNA selection during translation in bacteria. Here, we study the timing and control of reactions that occur during 70S IC formation by rapid kinetic techniques, using a toolbox of fluorescence-labeled translation components. We present a kinetic model based on global fitting of time courses obtained with eight different reporters at increasing concentrations of 50S subunits. IF1 and IF3 together affect the kinetics of subunit joining, but do not alter the elemental rates of subsequent steps of 70S IC maturation. After 50S subunit joining, IF2-dependent reactions take place independent of the presence of IF1 or IF3. GTP hydrolysis triggers the efficient dissociation of fMet-tRNA(fMet) from IF2 and promotes the dissociation of IF2 and IF1 from the 70S IC, but does not affect IF3. The presence of non-hydrolyzable GTP analogs shifts the equilibrium towards a stable 70S-mRNA-IF1-IF2-fMet-tRNA(fMet) complex. Our kinetic analysis reveals the molecular choreography of the late stages in translation initiation."],["dc.identifier.doi","10.1093/nar/gkv869"],["dc.identifier.gro","3141765"],["dc.identifier.isi","000371237600020"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/824"],["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","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","Directional transition from initiation to elongation in bacterial translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]