Boon, Kum-Loong

[["dc.bibliographiccitation.firstpage","2416"],["dc.bibliographiccitation.issue","23-24"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","2429"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Bao, Penghui"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2020-12-10T18:20:20Z"],["dc.date.available","2020-12-10T18:20:20Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1101/gad.308163.117"],["dc.identifier.eissn","1549-5477"],["dc.identifier.issn","0890-9369"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75524"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated B act complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","413"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","428"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Fourmann, Jean-Baptiste"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Christian, Henning"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2017-09-07T11:47:49Z"],["dc.date.available","2017-09-07T11:47:49Z"],["dc.date.issued","2013"],["dc.description.abstract","The spliceosome is a single-turnover enzyme that needs to be dismantled after catalysis to both release the mRNA and recycle small nuclear ribonucleoproteins (snRNPs) for subsequent rounds of pre-mRNA splicing. The RNP remodeling events occurring during spliceosome disassembly are poorly understood, and the composition of the released snRNPs are only roughly known. Using purified components in vitro, we generated post-catalytic spliceosomes that can be dissociated into mRNA and the intron-lariat spliceosome (ILS) by addition of the RNA helicase Prp22 plus ATP and without requiring the step 2 proteins Slu7 and Prp18. Incubation of the isolated ILS with the RNA helicase Prp43 plus Ntr1/Ntr2 and ATP generates defined spliceosomal dissociation products: the intron-lariat, U6 snRNA, a 20-25S U2 snRNP containing SF3a/b, an 18S U5 snRNP, and the \"nineteen complex\" associated with both the released U2 snRNP and intron-lariat RNA. Our system reproduces the entire ordered disassembly phase of the spliceosome with purified components, which defines the minimum set of agents required for this process. It enabled us to characterize the proteins of the ILS by mass spectrometry and identify the ATPase action of Prp43 as necessary and sufficient for dissociation of the ILS without the involvement of Brr2 ATPase."],["dc.identifier.doi","10.1101/gad.207779.112"],["dc.identifier.gro","3142392"],["dc.identifier.isi","000315286300007"],["dc.identifier.pmid","23431055"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7774"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 860]; GGNB (DFG) [GSC 226/1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0890-9369"],["dc.title","Dissection of the factor requirements for spliceosome disassembly and the elucidation of its dissociation products using a purified splicing system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","209"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Heininger, A. U."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Andreou, Alexandra-Zoi"],["dc.contributor.author","Boon, K.-L."],["dc.contributor.author","Prior, M."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:54:51Z"],["dc.date.available","2018-11-07T09:54:51Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362570603174"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36625"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Sequestering and protein cofactor competition regulate a multifunctional RNA helicase in different pathways"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1064"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","1070"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Kramer, Katharina"],["dc.contributor.author","Sachsenberg, Timo"],["dc.contributor.author","Beckmann, Benedikt M."],["dc.contributor.author","Qamar, Saadia"],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Hentze, Matthias W."],["dc.contributor.author","Kohlbacher, Oliver"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2018-11-07T09:34:34Z"],["dc.date.available","2018-11-07T09:34:34Z"],["dc.date.issued","2014"],["dc.description.abstract","RNA-protein complexes play pivotal roles in many central biological processes. Although methods based on high-throughput sequencing have advanced our ability to identify the specific RNAs bound by a particular protein, there is a need for precise and systematic ways to identify RNA interaction sites on proteins. We have developed an experimental and computational workflow combining photo-induced cross-linking, high-resolution mass spectrometry and automated analysis of the resulting mass spectra for the identification of cross-linked peptides, cross-linking sites and the cross-linked RNA oligonucleotide moieties of such RNA-binding proteins. The workflow can be applied to any RNA-protein complex of interest or to whole proteomes. We applied the approach to human and yeast mRNA-protein complexes in vitro and in vivo, demonstrating its powerful utility by identifying 257 cross-linking sites on 124 distinct RNA-binding proteins. The open-source software pipeline developed for this purpose, RNPxl, is available as part of the OpenMS project."],["dc.identifier.doi","10.1038/NMETH.3092"],["dc.identifier.isi","000342719100027"],["dc.identifier.pmid","25173706"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32197"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","320"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Heininger, Annika U."],["dc.contributor.author","Hackert, Phillip"],["dc.contributor.author","Andreou, Alexandra Z."],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.identifier.doi","10.1080/15476286.2016.1142038"],["dc.identifier.gro","3141714"],["dc.identifier.isi","000372909600008"],["dc.identifier.pmid","26821976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/258"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways"],["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"]]