Monecke, Thomas

[["dc.bibliographiccitation.firstpage","960"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","965"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Voss, Bela"],["dc.contributor.author","Russek, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Thomson, Emma"],["dc.contributor.author","Hurt, Ed"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-beta superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal a-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1-Ran-Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo."],["dc.identifier.doi","10.1073/pnas.1215214110"],["dc.identifier.gro","3142406"],["dc.identifier.isi","000313909100042"],["dc.identifier.pmid","23277578"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7930"],["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","0027-8424"],["dc.title","Structural basis for cooperativity of CRM1 export complex formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1087"],["dc.bibliographiccitation.issue","5930"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1091"],["dc.bibliographiccitation.volume","324"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Guettler, Thomas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Goerlich, Dirk"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:47:28Z"],["dc.date.available","2017-09-07T11:47:28Z"],["dc.date.issued","2009"],["dc.description.abstract","CRM1 mediates nuclear export of numerous unrelated cargoes, which may carry a short leucine-rich nuclear export signal or export signatures that include folded domains. How CRM1 recognizes such a variety of cargoes has been unknown up to this point. Here we present the crystal structure of the SPN1.CRM1.RanGTP export complex at 2.5 angstrom resolution (where SPN1 is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran). SPN1 is a nuclear import adapter for cytoplasmically assembled, m(3)G-capped spliceosomal U snRNPs (small nuclear ribonucleoproteins). The structure shows how CRM1 can specifically return the cargo-free form of SPN1 to the cytoplasm. The extensive contact area includes five hydrophobic residues at the SPN1 amino terminus that dock into a hydrophobic cleft of CRM1, as well as numerous hydrophilic contacts of CRM1 to m3G cap-binding domain and carboxyl-terminal residues of SPN1. The structure suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin."],["dc.identifier.doi","10.1126/science.1173388"],["dc.identifier.gro","3143116"],["dc.identifier.isi","000266246700046"],["dc.identifier.pmid","19389996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/595"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","0036-8075"],["dc.title","Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","s30"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica. Section A, Foundations and Advances"],["dc.bibliographiccitation.lastpage","s31"],["dc.bibliographiccitation.volume","66"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Güttler, Thomas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Doelker, Nicole"],["dc.contributor.author","Blanchet, Clement"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Görlich, Dirk"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Svergun, Dmitri"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2021-03-05T08:58:57Z"],["dc.date.available","2021-03-05T08:58:57Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1107/S0108767310099319"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80313"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0108-7673"],["dc.title","Structural basis for CRM1 nuclear export complex assembly"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","68a"],["dc.bibliographiccitation.issue","2, Supplement 1"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Voß, Bela"],["dc.contributor.author","Russek, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Thomson, Emma"],["dc.contributor.author","Hurt, Ed"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2018-05-28T11:48:46Z"],["dc.date.available","2018-05-28T11:48:46Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.411"],["dc.identifier.uri","http://hdl.handle.net/2/14783"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Structural Determinants of Conformational Flexibility and Long-Range Allostery of the CRM1 Export Complex"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","923"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","930"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Liu, Yi"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Kuhle, Bernhard"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Schell, Stephanie"],["dc.contributor.author","Chari, Ashwin"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:46:12Z"],["dc.date.available","2017-09-07T11:46:12Z"],["dc.date.issued","2014"],["dc.description.abstract","The multisubunit eukaryotic translation initiation factor 3, among which the subunit b (eIF3b) is a major scaffold protein, plays essential roles in protein synthesis. Here, we report the crystal structure of the WD40 domain of Chaetomium thermophilum eIF3b, revealing a nine-bladed beta-propeller fold. Sequence analysis indicates that this propeller architecture is common to all eIF3b orthologs. Revisiting the cryo-electron microscopy (cryo-EM) map of the 43S preinitiation complex suggests an interaction of the eIF3b with the 40S ribosomal subunit involving the ribosomal protein S9e and the 18S rRNA. This model is strongly supported by the direct binding of eIF3b to 40S ribosomes and to the isolated ribosomal protein rpS9e in vitro."],["dc.identifier.doi","10.1016/j.str.2014.03.010"],["dc.identifier.gro","3142106"],["dc.identifier.isi","000338206200014"],["dc.identifier.pmid","24768115"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4611"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [CH1098/1-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1878-4186"],["dc.relation.issn","0969-2126"],["dc.title","Translation Initiation Factor eIF3b Contains a Nine-Bladed β-Propeller and Interacts with the 40S Ribosomal Subunit"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1367"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U229"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Guettler, Thomas"],["dc.contributor.author","Madl, Tobias"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Deichsel, Danilo"],["dc.contributor.author","Corsini, Lorenzo"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Sattler, Michael"],["dc.contributor.author","Goerlich, Dirk"],["dc.date.accessioned","2017-09-07T11:45:15Z"],["dc.date.available","2017-09-07T11:45:15Z"],["dc.date.issued","2010"],["dc.description.abstract","Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP-CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Phi) residues, yet CRM1 recognizes them with the same rigid set of five Phi pockets. The different Phi spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an alpha-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Phi pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly."],["dc.identifier.doi","10.1038/nsmb.1931"],["dc.identifier.gro","3142839"],["dc.identifier.isi","000283773200015"],["dc.identifier.pmid","20972448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/287"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1545-9993"],["dc.title","NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e90915"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.lastpage","13"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Buschmann, Juliane"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Wahle, Elmar"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:46:28Z"],["dc.date.available","2017-09-07T11:46:28Z"],["dc.date.issued","2014"],["dc.description.abstract","5'-nucleotidases catalyze the hydrolytic dephosphorylation of nucleoside monophosphates. As catabolic enzymes they contribute significantly to the regulation of cellular nucleotide levels; misregulation of nucleotide metabolism and nucleotidase deficiencies are associated with a number of diseases. The seven human 5'-nucleotidases differ with respect to substrate specificity and cellular localization. Recently, the novel cytosolic 5'-nucleotidase III-like protein, or cN-IIIB, has been characterized in human and Drosophila. cN-IIIB exhibits a strong substrate preference for the modified nucleotide 7-methylguanosine monophosphate but the structural reason for this preference was unknown. Here, we present crystal structures of cN-IIIB from Drosophila melanogaster bound to the reaction products 7-methylguanosine or cytidine. The structural data reveal that the cytosine-and 7-methylguanine moieties of the products are stacked between two aromatic residues in a coplanar but off-centered position. 7-methylguanosine is specifically bound through p-p interactions and distinguished from unmodified guanosine by additional cation-p coulomb interactions between the aromatic side chains and the positively charged 7-methylguanine. Notably, the base is further stabilized by T-shaped edge-to-face stacking of an additional tryptophan packing perpendicularly against the purine ring and forming, together with the other aromates, an aromatic slot. The structural data in combination with site-directed mutagenesis experiments reveal the molecular basis for the broad substrate specificity of cN-IIIB but also explain the substrate preference for 7-methylguanosine monophosphate. Analyzing the substrate specificities of cN-IIIB and the main pyrimidine 59-nucleotidase cN-IIIA by mutagenesis studies, we show that cN-IIIA dephosphorylates the purine m(7)GMP as well, hence redefining its substrate spectrum. Docking calculations with cN-IIIA and m(7)GMP as well as biochemical data reveal that Asn69 does not generally exclude the turnover of purine substrates thus correcting previous suggestions."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pone.0090915"],["dc.identifier.gro","3142174"],["dc.identifier.isi","000332483600105"],["dc.identifier.pmid","24603684"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5355"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Gottingen University; DFG"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Crystal Structures of the Novel Cytosolic 5'-Nucleotidase IIIB Explain Its Preference for m7GMP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]