Tauchert, Marcel J.

[["dc.bibliographiccitation.firstpage","705"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta crystallographica. Section D, Structural biology"],["dc.bibliographiccitation.lastpage","717"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Hémonnot, Clément"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:04Z"],["dc.date.available","2020-12-10T18:26:04Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotic cells, the exchange of macromolecules between the nucleus and cytoplasm is highly selective and requires specialized soluble transport factors. Many of them belong to the importin-beta superfamily, the members of which share an overall superhelical structure owing to the tandem arrangement of a specific motif, the HEAT repeat. This structural organization leads to great intrinsic flexibility, which in turn is a prerequisite for the interaction with a variety of proteins and for its transport function. During the passage from the aqueous cytosol into the nucleus, the receptor passes the gated channel of the nuclear pore complex filled with a protein meshwork of unknown organization, which seems to be highly selective owing to the presence of FG-repeats, which are peptides with hydrophobic patches. Here, the structural changes of free importin-beta from a single organism, crystallized in polar (salt) or apolar (PEG) buffer conditions, are reported. This allowed analysis of the structural changes, which are attributable to the surrounding milieu and are not affected by bound interaction partners. The importin-beta structures obtained exhibit significant conformational changes and suggest an influence of the polarity of the environment, resulting in an extended conformation in the PEG condition. The significance of this observation is supported by SAXS experiments and the analysis of other crystal structures of importin-beta deposited in the Protein Data Bank."],["dc.identifier.doi","10.1107/S2059798316004940"],["dc.identifier.fs","622294"],["dc.identifier.gro","3141673"],["dc.identifier.isi","000379911500002"],["dc.identifier.issn","2059-7983"],["dc.identifier.pmid","27303791"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75940"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2059-7983"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of the crystallization condition on importin-β conformation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","112"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Acta Crystallographica Section F Structural Biology Communications"],["dc.bibliographiccitation.lastpage","120"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Fourmann, Jean-Baptiste"],["dc.contributor.author","Christian, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T18:26:00Z"],["dc.date.available","2020-12-10T18:26:00Z"],["dc.date.issued","2016"],["dc.description.abstract","RNA helicases are indispensable for all organisms in each domain of life and have implications in numerous cellular processes. The DEAH-box RNA helicase Prp43 is involved in pre-mRNA splicing as well as rRNA maturation. Here, the crystal structure of Chaetomium thermophilum Prp43 at 2.9 angstrom resolution is revealed. Furthermore, it is demonstrated that Prp43 from C. thermophilum is capable of functionally replacing its orthologue from Saccharomyces cerevisiae in spliceosomal disassembly assays."],["dc.identifier.doi","10.1107/S2053230X15024498"],["dc.identifier.eissn","2053-230X"],["dc.identifier.gro","3141733"],["dc.identifier.isi","000369384100004"],["dc.identifier.pmid","26841761"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75911"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Int Union Crystallography"],["dc.relation.issn","2053-230X"],["dc.title","Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","409"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Acta Crystallographica Section F Structural Biology Communications"],["dc.bibliographiccitation.lastpage","416"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T18:26:00Z"],["dc.date.available","2020-12-10T18:26:00Z"],["dc.date.issued","2016"],["dc.description.abstract","Prp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6.U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5'-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 angstrom resolution and is compared with the available structures of homologues."],["dc.identifier.doi","10.1107/S2053230X16006038"],["dc.identifier.eissn","2053-230X"],["dc.identifier.gro","3141693"],["dc.identifier.isi","000375852400011"],["dc.identifier.pmid","27139834"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75912"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Int Union Crystallography"],["dc.relation.issn","2053-230X"],["dc.title","Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]