Wahl, Markus C.

[["dc.bibliographiccitation.firstpage","791"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","802"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Luo, Xiao"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Bubunenko, Mikhail"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Court, Donald L."],["dc.contributor.author","Gottesman, Max E."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T11:07:50Z"],["dc.date.available","2018-11-07T11:07:50Z"],["dc.date.issued","2008"],["dc.description.abstract","Protein S10 is a component of the 30S ribosomal subunit and participates together with NusB protein in processive transcription antitermination. The molecular mechanisms by which S10 can act as a translation or a transcription factor are not understood. We used complementation assays and recombineering to delineate regions of S10 dispensable for antitermination, and determined the crystal structure of a transcriptionally active NusB-S10 complex. In this complex, S10 adopts the same fold as in the 30S subunit and is blocked from simultaneous association with the ribosome. Mass spectrometric mapping of UV-induced crosslinks revealed that the NusB-S10 complex presents an intermolecular, composite, and contiguous binding surface for RNAs containing BoxA antitermination signals. Furthermore, S10 overproduction complemented a nusB null phenotype. These data demonstrate that S10 and NusB together form a BoxA-binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination."],["dc.identifier.doi","10.1016/j.molcel.2008.10.028"],["dc.identifier.isi","000262184200009"],["dc.identifier.pmid","19111659"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52668"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-2765"],["dc.title","Structural and Functional Analysis of the E. coli NusB-S10 Transcription Antitermination Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20"],["dc.bibliographiccitation.issue","S1"],["dc.bibliographiccitation.journal","Der Nervenarzt"],["dc.bibliographiccitation.lastpage","21"],["dc.bibliographiccitation.volume","81"],["dc.contributor.author","Jung, P."],["dc.contributor.author","Wibral, Michael"],["dc.contributor.author","Bliem, B."],["dc.contributor.author","Lu, M.-K."],["dc.contributor.author","Wahl, M."],["dc.contributor.author","Ziemann, U."],["dc.date.accessioned","2022-06-08T07:59:06Z"],["dc.date.available","2022-06-08T07:59:06Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1007/s00115-010-3143-0"],["dc.identifier.pii","3143"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110635"],["dc.language.iso","de"],["dc.notes.intern","DOI-Import GROB-575"],["dc.relation.eissn","1433-0407"],["dc.relation.issn","0028-2804"],["dc.title","Multimodale Evaluation des somatosensorischen CC bei Gesunden und Patienten mit früher RRMS"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2341"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","2348"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Ghalei, H."],["dc.contributor.author","Hsiao, H.-H."],["dc.contributor.author","Urlaub, H."],["dc.contributor.author","Wahl, M. C."],["dc.contributor.author","Watkins, N. J."],["dc.date.accessioned","2021-06-01T10:48:15Z"],["dc.date.available","2021-06-01T10:48:15Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1261/rna.2380410"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85870"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","1355-8382"],["dc.title","A novel Nop5-sRNA interaction that is required for efficient archaeal box C/D sRNP formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","531"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","541"],["dc.bibliographiccitation.volume","385"],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T08:33:29Z"],["dc.date.available","2018-11-07T08:33:29Z"],["dc.date.issued","2009"],["dc.description.abstract","The precursor mRNA retention and splicing (RES) complex mediates nuclear retention and enhances splicing of precursor mRNAs. The RES complex from yeast comprises three proteins, Snu17p, Bud13p and Pml1p. Snu17p acts as a central platform that concomitantly binds the Bud13p and Pml1p subunits via short peptide epitopes. As a step to decipher the molecular architecture of the RES complex, we have determined crystal structures of full-length Pml1p and N-terminally truncated Pml1p. The first 50 residues of full-length Pml1p, encompassing the Snu17p-binding region, are disordered, showing that Pml1p binds to Snu17p via an intrinsically unstructured region. The remainder of Pml1p folds as a forkhead-associated (FHA) domain, which is expanded by a number of noncanonical elements compared with known FHA domains from other proteins. An atypical N-terminal appendix runs across one beta-sheet and thereby stabilizes the domain as shown by deletion experiments. FHA domains are thought to constitute phosphopeptide-binding elements. Consistently, a sulfate ion was found at the putative phosphopeptide-binding loops of full-length Pml1p. The N-terminally truncated version of the protein lacked a similar phosphopeptide mimic but retained an almost identical structure. A long loop neighboring the putative phosphopeptide-binding site was disordered in both structures. Comparison with other FHA domain proteins suggests that this loop adopts a defined conformation upon ligand binding and thereby confers ligand specificity. Our results show that in the RES complex, an FHA domain of Pml1p is flexibly tethered via an unstructured N-terminal region to Snu17p. (C) 2008 Elsevier Ltd. All rights reserved."],["dc.description.sponsorship","Max Planck Society"],["dc.identifier.doi","10.1016/j.jmb.2008.10.087"],["dc.identifier.isi","000262916900016"],["dc.identifier.pmid","19010333"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17588"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Crystal Structure of the Pml1p Subunit of the Yeast Precursor mRNA Retention and Splicing Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","S002192582100627X"],["dc.bibliographiccitation.firstpage","100829"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.volume","297"],["dc.contributor.author","Absmeier, Eva"],["dc.contributor.author","Vester, Karen"],["dc.contributor.author","Ghane, Tahereh"],["dc.contributor.author","Burakovskiy, Dmitry"],["dc.contributor.author","Milon, Pohl"],["dc.contributor.author","Imhof, Petra"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Santos, Karine F."],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2022-03-01T11:45:11Z"],["dc.date.available","2022-03-01T11:45:11Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.jbc.2021.100829"],["dc.identifier.pii","S002192582100627X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103241"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0021-9258"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Long-range allostery mediates cooperative adenine nucleotide binding by the Ski2-like RNA helicase Brr2"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","328"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","339"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Mukherjee, Konark"],["dc.contributor.author","Sharma, Manu"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bourenkov, Gleb P."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Suedhof, Thomas C."],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T11:16:02Z"],["dc.date.available","2018-11-07T11:16:02Z"],["dc.date.issued","2008"],["dc.description.abstract","CASK is a unique MAGUK protein that contains an N-terminal CaM-kinase domain besides the typical MAGUK domains. The CASK CaM-kinase domain is presumed to be a catalytically inactive pseudokinase because it lacks the canonical DFG motif required for Mg2+ binding that is thought to be indispensable for kinase activity. Here we show, however, that CASK functions as an active protein kinase even without Mg2+ binding. High-resolution crystal structures reveal that the CASK CaM-kinase domain adopts a constitutively active conformation that binds ATP and catalyzes phosphotransfer without Mg2+. The CASK CaM-kinase domain phosphorylates itself and at least one physiological interactor, the synaptic protein neurexin-1, to which CASK is recruited via its PDZ domain. Thus, our data indicate that CASK combines the scaffolding activity of MAGUKs with an unusual kinase activity that phosphorylates substrates recuited by the scaffolding activity. Moreover, our study suggests that other pseudokinases (10% of the kinome) could also be catalytically active."],["dc.description.sponsorship","NIMH NIH HHS [R37 MH052804, R37 MH052804-08, R37 MH52804-08]"],["dc.identifier.doi","10.1016/j.cell.2008.02.036"],["dc.identifier.isi","000255052000021"],["dc.identifier.pmid","18423203"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54500"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","0092-8674"],["dc.title","CASK functions as a Mg2+-independent neurexin kinase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13005"],["dc.bibliographiccitation.issue","32"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13009"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:49:26Z"],["dc.date.available","2017-09-07T11:49:26Z"],["dc.date.issued","2007"],["dc.description.abstract","Dronpa is a novel GFP-like fluorescent protein with exceptional light-controlled switching properties. It may be reversibly switched between a fluorescent on-state and a nonfluorescent off-state by irradiation with light. To elucidate the molecular basis of the switching mechanism, we generated reversibly switchable Dronpa protein crystals. Using these crystals we determined the elusive dark-state structure of Dronpa at 1.95-angstrom resolution. We found that the photoswitching results in a cis-trans isomerization of the chromophore accompanied by complex structural rearrangements of four nearby amino acid residues. Because of this cascade of intramolecular events, the chromophore is exposed to distinct electrostatic surface potentials, which are likely to influence the protonation equilibria at the chromophore. We suggest a comprehensive model for the light-induced switching mechanism, connecting a cascade of structural rearrangements with different protonation states of the chromophore."],["dc.identifier.doi","10.1073/pnas.0700629104"],["dc.identifier.gro","3143453"],["dc.identifier.isi","000248650300011"],["dc.identifier.pmid","17646653"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/969"],["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 reversible photoswitching in Dronpa"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","32317"],["dc.bibliographiccitation.issue","47"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","32327"],["dc.bibliographiccitation.volume","283"],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T11:08:57Z"],["dc.date.available","2018-11-07T11:08:57Z"],["dc.date.issued","2008"],["dc.description.abstract","The yeast pre-mRNA retention and splicing complex counteracts the escape of unspliced pre-mRNAs from the nucleus and activates splicing of a subset of Mer1p-dependent genes. A homologous complex is present in activated human spliceosomes. In many components of the spliceosome, RNA recognition motifs (RRMs) serve as versatile protein-RNA or protein-protein interaction platforms. Here, we show that in the retention and splicing complex, an atypical RRM of the Snu17p (small nuclear ribonucleoprotein-associated protein 17) subunit acts as a scaffold that organizes the other two constituents, Bud13p (bud site selection 13) and Pml1p (pre-mRNA leakage 1). GST pull-down experiments and size exclusion chromatography revealed that Snu17p constitutes the central platform of the complex, whereas Bud13p and Pml1p do not interact with each other. Fluorimetric structure probing showed the entire Bud13p and the N-terminal third of Pml1p to be natively disordered in isolation. Mutational analysis and tryptophan fluorescence confirmed that a conserved tryptophan-containing motif in the C terminus of Bud13p binds to the core RRM of Snu17p, whereas a different interaction surface encompassing a C-terminal extension of the Snu17p RRM is required to bind an N-terminal peptide of Pml1p. Isothermal titration calorimetry revealed 1: 1 interaction stoichiometries, large negative binding entropies, and dissociation constants in the low nanomolar and micromolar ranges for the Snu17p-Bud13p and the Snu17p-Pml1p interactions, respectively. Our results demonstrate that the noncanonical Snu17p RRM concomitantly binds multiple ligand proteins via short, intrinsically unstructured peptide epitopes and thereby acts as a platform that displays functional modules of the ligands, such as a forkhead-associated domain of Pml1p and a conserved polylysine motif of Bud13p."],["dc.description.sponsorship","Max-Planck-Society"],["dc.identifier.doi","10.1074/jbc.M804977200"],["dc.identifier.isi","000260893700018"],["dc.identifier.pmid","18809678"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52909"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","An Unusual RNA Recognition Motif Acts as a Scaffold for Multiple Proteins in the Pre-mRNA Retention and Splicing Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Jia, Junqiao"],["dc.contributor.author","Absmeier, Eva"],["dc.contributor.author","Holton, Nicole"],["dc.contributor.author","Pietrzyk-Brzezinska, Agnieszka J."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2021-04-14T08:31:48Z"],["dc.date.available","2021-04-14T08:31:48Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-19221-x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83718"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.title","The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Protein Science / Supplement"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Brakemann, Tanja"],["dc.contributor.author","Stiel, Andre C."],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:45:52Z"],["dc.date.available","2017-09-07T11:45:52Z"],["dc.date.issued","2012"],["dc.format.extent","164"],["dc.identifier.gro","3145551"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3261"],["dc.notes.intern","lifescience"],["dc.notes.status","public"],["dc.notes.submitter","oschaef1"],["dc.relation.eissn","1469-896X"],["dc.relation.issn","0961-8368"],["dc.title","Dreiklang - the one, two, three in photoswitching"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]