Maracci, Cristina

[["dc.bibliographiccitation.firstpage","752"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","757"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Florin, Tanja"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Graf, Michael"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Klepacki, Dorota"],["dc.contributor.author","Berninghausen, Otto"],["dc.contributor.author","Beckmann, Roland"],["dc.contributor.author","Vázquez-Laslop, Nora"],["dc.contributor.author","Wilson, Daniel N."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Mankin, Alexander S."],["dc.date.accessioned","2018-01-24T13:03:20Z"],["dc.date.available","2018-01-24T13:03:20Z"],["dc.date.issued","2017"],["dc.description.abstract","Many antibiotics stop bacterial growth by inhibiting different steps of protein synthesis. However, no specific inhibitors of translation termination are known. Proline-rich antimicrobial peptides, a component of the antibacterial defense system of multicellular organisms, interfere with bacterial growth by inhibiting translation. Here we show that Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination."],["dc.identifier.doi","10.1038/nsmb.3439"],["dc.identifier.pmid","28741611"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11795"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1545-9985"],["dc.title","An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Carney, Travis D"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Yatsenko, Andriy S"],["dc.contributor.author","Shcherbata, Halyna R"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-01-11T14:08:08Z"],["dc.date.available","2022-01-11T14:08:08Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Translational readthrough (TR) occurs when the ribosome decodes a stop codon as a sense codon, resulting in two protein isoforms synthesized from the same mRNA. TR has been identified in several eukaryotic organisms; however, its biological significance and mechanism remain unclear. Here, we quantify TR of several candidate genes in Drosophila melanogaster and characterize the regulation of TR in the large Maf transcription factor Traffic jam (Tj). Using CRISPR/Cas9-generated mutant flies, we show that the TR-generated Tj isoform is expressed in a subset of neural cells of the central nervous system and is excluded from the somatic cells of gonads. Control of TR in Tj is critical for preservation of neuronal integrity and maintenance of reproductive health. The tissue-specific distribution of a release factor splice variant, eRF1H, plays a critical role in modulating differential TR of leaky stop codon contexts. Fine-tuning of gene regulatory functions of transcription factors by TR provides a potential mechanism for cell-specific regulation of gene expression."],["dc.description.abstract","Abstract Translational readthrough (TR) occurs when the ribosome decodes a stop codon as a sense codon, resulting in two protein isoforms synthesized from the same mRNA. TR has been identified in several eukaryotic organisms; however, its biological significance and mechanism remain unclear. Here, we quantify TR of several candidate genes in Drosophila melanogaster and characterize the regulation of TR in the large Maf transcription factor Traffic jam (Tj). Using CRISPR/Cas9-generated mutant flies, we show that the TR-generated Tj isoform is expressed in a subset of neural cells of the central nervous system and is excluded from the somatic cells of gonads. Control of TR in Tj is critical for preservation of neuronal integrity and maintenance of reproductive health. The tissue-specific distribution of a release factor splice variant, eRF1H, plays a critical role in modulating differential TR of leaky stop codon contexts. Fine-tuning of gene regulatory functions of transcription factors by TR provides a potential mechanism for cell-specific regulation of gene expression."],["dc.identifier.doi","10.1093/nar/gkab1189"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97941"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-507"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0/"],["dc.title","Tissue-specific regulation of translational readthrough tunes functions of the traffic jam transcription factor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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","463"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biopolymers"],["dc.bibliographiccitation.lastpage","475"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:44:48Z"],["dc.date.available","2017-09-07T11:44:48Z"],["dc.date.issued","2016"],["dc.description.abstract","Translational GTPases (trGTPases) play key roles in facilitating protein synthesis on the ribosome. Despite the high degree of evolutionary conservation in the sequences of their GTP-binding domains, the rates of GTP hydrolysis and nucleotide exchange vary broadly between different trGTPases. EF-Tu, one of the best-characterized model G proteins, evolved an exceptionally rapid and tightly regulated GTPase activity, which ensures rapid and accurate incorporation of amino acids into the nascent chain. Other trGTPases instead use the energy of GTP hydrolysis to promote movement or to ensure the forward commitment of translation reactions. Recent data suggest the GTPase mechanism of EF-Tu and provide an insight in the catalysis of GTP hydrolysis by its unusual activator, the ribosome. Here we summarize these advances in understanding the functional cycle and the regulation of trGTPases, stimulated by the elucidation of their structures on the ribosome and the progress in dissecting the reaction mechanism of GTPases. (C) 2016 The Authors. Biopolymers Published by Wiley Periodicals, Inc."],["dc.identifier.doi","10.1002/bip.22832"],["dc.identifier.gro","3141650"],["dc.identifier.isi","000379166800005"],["dc.identifier.pmid","26971860"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5343"],["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","1097-0282"],["dc.relation.issn","0006-3525"],["dc.title","Translational GTPases"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","20160182"],["dc.bibliographiccitation.issue","1716"],["dc.bibliographiccitation.journal","Philosophical Transactions B"],["dc.bibliographiccitation.volume","372"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2018-01-17T12:54:50Z"],["dc.date.available","2018-01-17T12:54:50Z"],["dc.date.issued","2017"],["dc.description.abstract","Elongation factors Tu (EF-Tu) and SelB are translational GTPases that deliver aminoacyl-tRNAs (aa-tRNAs) to the ribosome. In each canonical round of translation elongation, aa-tRNAs, assisted by EF-Tu, decode mRNA codons and insert the respective amino acid into the growing peptide chain. Stop codons usually lead to translation termination; however, in special cases UGA codons are recoded to selenocysteine (Sec) with the help of SelB. Recruitment of EF-Tu and SelB together with their respective aa-tRNAs to the ribosome is a multistep process. In this review, we summarize recent progress in understanding the role of ribosome dynamics in aa-tRNA selection. We describe the path to correct codon recognition by canonical elongator aa-tRNA and Sec-tRNASec and discuss the local and global rearrangements of the ribosome in response to correct and incorrect aa-tRNAs. We present the mechanisms of GTPase activation and GTP hydrolysis of EF-Tu and SelB and summarize what is known about the accommodation of aa-tRNA on the ribosome after its release from the elongation factor. We show how ribosome dynamics ensures high selectivity for the cognate aa-tRNA and suggest that conformational fluctuations, induced fit and kinetic discrimination play major roles in maintaining the speed and fidelity of translation.This article is part of the themed issue 'Perspectives on the ribosome'."],["dc.format.extent","1-10"],["dc.identifier.doi","10.1098/rstb.2016.0182"],["dc.identifier.pmid","28138068"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11694"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1471-2970"],["dc.subject","ribosome; tRNA; translation; decoding; recoding"],["dc.title","Ribosome dynamics during decoding"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3053"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Graf, Michael"],["dc.contributor.author","Huter, Paul"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Peterek, Miroslav"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wilson, Daniel N."],["dc.date.accessioned","2022-03-01T11:45:57Z"],["dc.date.available","2022-03-01T11:45:57Z"],["dc.date.issued","2018"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (German Research Foundation)"],["dc.identifier.doi","10.1038/s41467-018-05465-1"],["dc.identifier.pii","5465"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103509"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2041-1723"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","609"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","615"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Milón, Pohl"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Filonava, Liudmila"],["dc.contributor.author","Gualerzi, Claudio O."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T12:51:27Z"],["dc.date.available","2018-01-29T12:51:27Z"],["dc.date.issued","2012"],["dc.description.abstract","Initiation factors guide the ribosome in the selection of mRNA and translational reading frame. We determined the kinetically favored assembly pathway of the 30S preinitiation complex (30S PIC), an early intermediate in 30S initiation complex formation in Escherichia coli. IF3 and IF2 are the first factors to arrive, forming an unstable 30S-IF2-IF3 complex. Subsequently, IF1 joins and locks the factors in a kinetically stable 30S PIC to which fMet-tRNA(fMet) is recruited. Binding of mRNA is independent of initiation factors and can take place at any time during 30S PIC assembly, depending on the cellular concentration of the mRNA and the structural determinants at the ribosome-binding site. The kinetic analysis shows both specific and cumulative effects of initiation factors as well as kinetic checkpoints of mRNA selection at the entry into translation."],["dc.identifier.doi","10.1038/nsmb.2285"],["dc.identifier.pmid","22562136"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11883"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1545-9985"],["dc.title","Real-time assembly landscape of bacterial 30S translation initiation complex"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1056"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","1067"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Korniy, Natalia"],["dc.contributor.author","Klimova, Mariia"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Peng, Bee-Zen"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Belardinelli, Riccardo"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Peske, Frank"],["dc.date.accessioned","2022-03-01T11:46:50Z"],["dc.date.available","2022-03-01T11:46:50Z"],["dc.date.issued","2019"],["dc.description.abstract","Abstract During canonical translation, the ribosome moves along an mRNA from the start to the stop codon in exact steps of one codon at a time. The collinearity of the mRNA and the protein sequence is essential for the quality of the cellular proteome. Spontaneous errors in decoding or translocation are rare and result in a deficient protein. However, dedicated recoding signals in the mRNA can reprogram the ribosome to read the message in alternative ways. This review summarizes the recent advances in understanding the mechanisms of three types of recoding events: stop-codon readthrough, –1 ribosome frameshifting and translational bypassing. Recoding events provide insights into alternative modes of ribosome dynamics that are potentially applicable to other non-canonical modes of prokaryotic and eukaryotic translation."],["dc.description.abstract","Abstract During canonical translation, the ribosome moves along an mRNA from the start to the stop codon in exact steps of one codon at a time. The collinearity of the mRNA and the protein sequence is essential for the quality of the cellular proteome. Spontaneous errors in decoding or translocation are rare and result in a deficient protein. However, dedicated recoding signals in the mRNA can reprogram the ribosome to read the message in alternative ways. This review summarizes the recent advances in understanding the mechanisms of three types of recoding events: stop-codon readthrough, –1 ribosome frameshifting and translational bypassing. Recoding events provide insights into alternative modes of ribosome dynamics that are potentially applicable to other non-canonical modes of prokaryotic and eukaryotic translation."],["dc.identifier.doi","10.1093/nar/gkz783"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103816"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","Translational recoding: canonical translation mechanisms reinterpreted"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14418"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","14423"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Dannies, Ev"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:45:27Z"],["dc.date.available","2017-09-07T11:45:27Z"],["dc.date.issued","2014"],["dc.description.abstract","GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. The basic reaction mechanism and the way the ribosome contributes to catalysis are a matter of debate. Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Our data suggest that-contrary to current models-the reaction in free EF-Tu follows a pathway that does not involve the critical residue H84 in the switch II region. Binding to the ribosome without a cognate codon in the A site has little effect on the GTPase mechanism. In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K+ ions. We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the gamma-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome."],["dc.identifier.doi","10.1073/pnas.1412676111"],["dc.identifier.gro","3142034"],["dc.identifier.isi","000342633900039"],["dc.identifier.pmid","25246550"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3812"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [FOR 1805]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Ribosome-induced tuning of GTP hydrolysis by a translational GTPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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"]]