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","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","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.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"]]

[["dc.bibliographiccitation.firstpage","e2100370118"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Grass, Lena M."],["dc.contributor.author","Wollenhaupt, Jan"],["dc.contributor.author","Barthel, Tatjana"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Loll, Bernhard"],["dc.contributor.author","Klauck, Eberhard"],["dc.contributor.author","Antelmann, Haike"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2021-09-01T06:42:15Z"],["dc.date.available","2021-09-01T06:42:15Z"],["dc.date.issued","2021"],["dc.description.abstract","Many bacteria harbor RNA-dependent nucleoside-triphosphatases of the DEAH/RHA family, whose molecular mechanisms and cellular functions are poorly understood. Here, we show that the Escherichia coli DEAH/RHA protein, HrpA, is an ATP-dependent 3 to 5′ RNA helicase and that the RNA helicase activity of HrpA influences bacterial survival under antibiotics treatment. Limited proteolysis, crystal structure analysis, and functional assays showed that HrpA contains an N-terminal DEAH/RHA helicase cassette preceded by a unique N-terminal domain and followed by a large C-terminal region that modulates the helicase activity. Structures of an expanded HrpA helicase cassette in the apo and RNA-bound states in combination with cross-linking/mass spectrometry revealed ratchet-like domain movements upon RNA engagement, much more pronounced than hitherto observed in related eukaryotic DEAH/RHA enzymes. Structure-based functional analyses delineated transient interdomain contact sites that support substrate loading and unwinding, suggesting that similar conformational changes support RNA translocation. Consistently, modeling studies showed that analogous dynamic intramolecular contacts are not possible in the related but helicase-inactive RNA-dependent nucleoside-triphosphatase, HrpB. Our results indicate that HrpA may be an interesting target to interfere with bacterial tolerance toward certain antibiotics and suggest possible interfering strategies."],["dc.description.abstract","Many bacteria harbor RNA-dependent nucleoside-triphosphatases of the DEAH/RHA family, whose molecular mechanisms and cellular functions are poorly understood. Here, we show that the Escherichia coli DEAH/RHA protein, HrpA, is an ATP-dependent 3 to 5′ RNA helicase and that the RNA helicase activity of HrpA influences bacterial survival under antibiotics treatment. Limited proteolysis, crystal structure analysis, and functional assays showed that HrpA contains an N-terminal DEAH/RHA helicase cassette preceded by a unique N-terminal domain and followed by a large C-terminal region that modulates the helicase activity. Structures of an expanded HrpA helicase cassette in the apo and RNA-bound states in combination with cross-linking/mass spectrometry revealed ratchet-like domain movements upon RNA engagement, much more pronounced than hitherto observed in related eukaryotic DEAH/RHA enzymes. Structure-based functional analyses delineated transient interdomain contact sites that support substrate loading and unwinding, suggesting that similar conformational changes support RNA translocation. Consistently, modeling studies showed that analogous dynamic intramolecular contacts are not possible in the related but helicase-inactive RNA-dependent nucleoside-triphosphatase, HrpB. Our results indicate that HrpA may be an interesting target to interfere with bacterial tolerance toward certain antibiotics and suggest possible interfering strategies."],["dc.identifier.doi","10.1073/pnas.2100370118"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89016"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.title","Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","942"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nature Biotechnology"],["dc.bibliographiccitation.lastpage","U132"],["dc.bibliographiccitation.volume","29"],["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","Grotjohann, Tim"],["dc.contributor.author","Leutenegger, Marcel"],["dc.contributor.author","Plessmann, Uwe"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:43:22Z"],["dc.date.available","2017-09-07T11:43:22Z"],["dc.date.issued","2011"],["dc.description.abstract","Photoswitchable fluorescent proteins have enabled new approaches for imaging cells, but their utility has been limited either because they cannot be switched repeatedly or because the wavelengths for switching and fluorescence imaging are strictly coupled. We report a bright, monomeric, reversibly photoswitchable variant of GFP, Dreiklang, whose fluorescence excitation spectrum is decoupled from that for optical switching. Reversible on-and-off switching in living cells is accomplished at illumination wavelengths of similar to 365 nm and similar to 405 nm, respectively, whereas fluorescence is elicited at similar to 515 nm. Mass spectrometry and high-resolution crystallographic analysis of the same protein crystal in the photoswitched on- and off-states demonstrate that switching is based on a reversible hydration/dehydration reaction that modifies the chromophore. The switching properties of Dreiklang enable far-field fluorescence nanoscopy in living mammalian cells using both a coordinate-targeted and a stochastic single molecule switching approach."],["dc.identifier.doi","10.1038/nbt.1952"],["dc.identifier.gro","3142656"],["dc.identifier.isi","000296273000022"],["dc.identifier.pmid","21909082"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84"],["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.eissn","1546-1696"],["dc.relation.issn","1087-0156"],["dc.title","A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7922"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","7937"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Henning, Lisa M."],["dc.contributor.author","Santos, Karine F."],["dc.contributor.author","Sticht, Jana"],["dc.contributor.author","Jehle, Stefanie"],["dc.contributor.author","Lee, Chung-Tien"],["dc.contributor.author","Wittwer, Malte"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Stelzl, Ulrich"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Freund, Christian"],["dc.date.accessioned","2020-12-10T18:19:34Z"],["dc.date.available","2020-12-10T18:19:34Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1093/nar/gkx535"],["dc.identifier.eissn","1362-4962"],["dc.identifier.issn","0305-1048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75296"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A new role for FBP21 as regulator of Brr2 helicase activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2576"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","2587"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Absmeier, Eva"],["dc.contributor.author","Wollenhaupt, Jan"],["dc.contributor.author","Mozaffari-Jovin, Sina"],["dc.contributor.author","Becke, Christian"],["dc.contributor.author","Lee, Chung-Tien"],["dc.contributor.author","Preussner, Marco"],["dc.contributor.author","Heyd, Florian"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.contributor.author","Santos, Karine F."],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2018-11-07T09:47:30Z"],["dc.date.available","2018-11-07T09:47:30Z"],["dc.date.issued","2015"],["dc.description.abstract","The Brr2 helicase provides the key remodeling activity for spliceosome catalytic activation, during which it disrupts the U4/U6 di-snRNP (small nuclear RNA protein), and its activity has to be tightly regulated. Brr2 exhibits an unusual architecture, including an similar to 500-residue N-terminal region, whose functions and molecular mechanisms are presently unknown, followed by a tandem array of structurally similar helicase units (cassettes), only the first of which is catalytically active. Here, we show by crystal structure analysis of full-length Brr2 in complex with a regulatory Jab1/MPN domain of the Prp8 protein and by cross-linking/mass spectrometry of isolated Brr2 that the Brr2 N-terminal region encompasses two folded domains and adjacent linear elements that clamp and interconnect the helicase cassettes. Stepwise N-terminal truncations led to yeast growth and splicing defects, reduced Brr2 association with U4/U6.U5 tri-snRNPs, and increased ATP-dependent disruption of the tri-snRNP, yielding U4/U6 disnRNP and U5 snRNP. Trends in the RNA-binding, ATPase, and helicase activities of the Brr2 truncation variants are fully rationalized by the crystal structure, demonstrating that the N-terminal region autoinhibits Brr2 via substrate competition and conformational clamping. Our results reveal molecular mechanisms that prevent premature and unproductive tri-snRNP disruption and suggest novel principles of Brr2-dependent splicing regulation."],["dc.identifier.doi","10.1101/gad.271528.115"],["dc.identifier.isi","000366758700005"],["dc.identifier.pmid","26637280"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12754"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35127"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1549-5477"],["dc.relation.issn","0890-9369"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nature Microbiology"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Said, Nelly"],["dc.contributor.author","Krupp, Ferdinand"],["dc.contributor.author","Anedchenko, Ekaterina"],["dc.contributor.author","Santos, Karine F."],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Huang, Yong-Heng"],["dc.contributor.author","Lee, Chung-Tien"],["dc.contributor.author","Loll, Bernhard"],["dc.contributor.author","Behrmann, Elmar"],["dc.contributor.author","Bürger, Jörg"],["dc.contributor.author","Mielke, Thorsten"],["dc.contributor.author","Loerke, Justus"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Spahn, Christian M. T."],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2020-12-10T18:09:31Z"],["dc.date.available","2020-12-10T18:09:31Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1038/nmicrobiol.2017.62"],["dc.identifier.eissn","2058-5276"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73678"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Structural basis for λN-dependent processive transcription antitermination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2422"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","2434"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Mozaffari-Jovin, Sina"],["dc.contributor.author","Santos, Karine F."],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Luehrmann, Reinhard"],["dc.date.accessioned","2018-11-07T09:04:02Z"],["dc.date.available","2018-11-07T09:04:02Z"],["dc.date.issued","2012"],["dc.description.abstract","The spliceosomal RNA helicase Brr2 catalyzes unwinding of the U4/U6 snRNA duplex, an essential step for spliceosome catalytic activation. Brr2 is regulated in part by the spliceosomal Prp8 protein by an unknown mechanism. We demonstrate that the RNase H (RH) domain of yeast Prp8 binds U4/U6 small nuclear RNA (snRNA) with the single-stranded regions of U4 and U6 preceding U4/U6 stem I, contributing to its binding. Via cross-linking coupled with mass spectrometry, we identify RH domain residues that contact the U4/U6 snRNA. We further demonstrate that the same single-stranded region of U4 preceding U4/U6 stem I is recognized by Brr2, indicating that it translocates along U4 and first unwinds stem I of the U4/U6 duplex. Finally, we show that the RH domain of Prp8 interferes with U4/U6 unwinding by blocking Brr2's interaction with the U4 snRNA. Our data reveal a novel mechanism whereby Prp8 negatively regulates Brr2 and potentially prevents premature U4/U6 unwinding during splicing. They also support the idea that the RH domain acts as a platform for the exchange of U6 snRNA for U1 at the 59 splice site. Our results provide insights into the mechanism whereby Brr2 unwinds U4/U6 and show how this activity is potentially regulated prior to spliceosome activation."],["dc.identifier.doi","10.1101/gad.200949.112"],["dc.identifier.isi","000310583900007"],["dc.identifier.pmid","23124066"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25022"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","0890-9369"],["dc.title","The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]