Haag, Sara

[["dc.bibliographiccitation.firstpage","1532"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1543"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Warda, Ahmed S."],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Guennigmann, Manuel A."],["dc.contributor.author","Hoebartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:52:51Z"],["dc.date.available","2018-11-07T09:52:51Z"],["dc.date.issued","2015"],["dc.description.abstract","Many cellular RNAs require modification of specific residues for their biogenesis, structure, and function. 5-methylcytosine (m(5)C) is a common chemical modification in DNA and RNA but in contrast to the DNA modifying enzymes, only little is known about the methyltransferases that establish m(5)C modifications in RNA. The putative RNA methyltransferase NSUN6 belongs to the family of Nol1/Nop2/SUN domain (NSUN) proteins, but so far its cellular function has remained unknown. To reveal the target spectrum of human NSUN6, we applied UV crosslinking and analysis of cDNA (CRAC) as well as chemical crosslinking with 5-azacytidine. We found that human NSUN6 is associated with tRNAs and acts as a tRNA methyltransferase. Furthermore, we uncovered tRNACys and tRNAThr as RNA substrates of NSUN6 and identified the cytosine C72 at the 3' end of the tRNA acceptor stem as the target nucleoside. Interestingly, target recognition in vitro depends on the presence of the 3'-CCA tail. Together with the finding that NSUN6 localizes to the cytoplasm and largely colocalizes with marker proteins for the Golgi apparatus and pericentriolar matrix, our data suggest that NSUN6 modifies tRNAs in a late step in their biogenesis."],["dc.identifier.doi","10.1261/rna.051524.115"],["dc.identifier.isi","000359996100002"],["dc.identifier.pmid","26160102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36208"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1469-9001"],["dc.relation.issn","1355-8382"],["dc.title","NSUN6 is a human RNA methyltransferase that catalyzes formation of m(5)C72 in specific tRNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","180"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","187"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T10:01:50Z"],["dc.date.available","2018-11-07T10:01:50Z"],["dc.date.issued","2015"],["dc.description.abstract","Ribosomal (r) RNAs are extensively modified during ribosome synthesis and their modification is required for the fidelity and efficiency of translation. Besides numerous small nucleolar RNA-guided 2'-O methylations and pseudouridinylations, a number of individual RNA methyltransferases are involved in rRNA modification. WBSCR22/Merm1, which is affected in Williams-Beuren syndrome and has been implicated in tumorigenesis and metastasis formation, was recently shown to be involved in ribosome synthesis, but its molecular functions have remained elusive. Here we show that depletion of WBSCR22 leads to nuclear accumulation of 3'-extended 18SE pre-rRNA intermediates resulting in impaired 18S rRNA maturation. We map the 3' ends of the 18SE pre-rRNA intermediates accumulating after depletion of WBSCR22 and in control cells using 3'-RACE and deep sequencing. Furthermore, we demonstrate that WBSCR22 is required for N-7-methylation of G1639 in human 18S rRNA in vivo. Interestingly, the catalytic activity of WBSCR22 is not required for 18S pre-rRNA processing, suggesting that the key role of WBSCR22 in 40S subunit biogenesis is independent of its function as an RNA methyltransferase."],["dc.identifier.doi","10.1261/rna.047910.114"],["dc.identifier.isi","000348036400004"],["dc.identifier.pmid","25525153"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38109"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1469-9001"],["dc.relation.issn","1355-8382"],["dc.title","WBSCR22/Merm1 is required for late nuclear pre-ribosomal RNA processing and mediates N-7-methylation of G1639 in human 18S rRNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","259"],["dc.bibliographiccitation.lastpage","268"],["dc.bibliographiccitation.seriesnr","1562"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.editor","Lusser, Alexandra"],["dc.date.accessioned","2021-06-02T10:44:25Z"],["dc.date.available","2021-06-02T10:44:25Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/978-1-4939-6807-7_17"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87031"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-6807-7"],["dc.relation.isbn","978-1-4939-6805-3"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","RNA Methylation : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1562"],["dc.title","In Vitro Assays for RNA Methyltransferase Activity"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","269"],["dc.bibliographiccitation.lastpage","281"],["dc.bibliographiccitation.seriesnr","1562"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.editor","Lusser, Alexandra"],["dc.date.accessioned","2021-06-02T10:44:25Z"],["dc.date.available","2021-06-02T10:44:25Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/978-1-4939-6807-7_18"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87032"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-6807-7"],["dc.relation.isbn","978-1-4939-6805-3"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","RNA Methylation : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1562"],["dc.title","Crosslinking Methods to Identify RNA Methyltransferase Targets In Vivo"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5353"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","5364"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Warda, Ahmed S."],["dc.contributor.author","Freytag, Bernard"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Goerlich, Dirk"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T10:04:27Z"],["dc.date.available","2018-11-07T10:04:27Z"],["dc.date.issued","2016"],["dc.description.abstract","Bowen-Conradi syndrome (BCS) is a severe genetic disorder that is characterised by various developmental abnormalities, bone marrow failure and early infant death. This disease is caused by a single mutation leading to the aspartate 86 to glycine (D86G) exchange in the essential nucleolar RNA methyltransferase EMG1. EMG1 is required for the synthesis of the small ribosomal subunit and is involved in modification of the 18S ribosomal RNA. Here, we identify the pre-ribosomal factors NOP14, NOC4L and UTP14A as members of a nucleolar subcomplex that contains EMG1 and is required for its recruitment to nucleoli. The BCS mutation in EMG1 leads to reduced nucleolar localisation, accumulation of EMG1(D86G) in nuclear foci and its proteasome-dependent degradation. We further show that EMG1 can be imported into the nucleus by the importins (Imp) Imp alpha/beta or Imp beta/7. Interestingly, in addition to its role in nuclear import, binding of the Imp beta/7 heterodimer can prevent unspecific aggregation of both EMG1 and EMG1(D86G) on RNAs in vitro, indicating that the importins act as chaperones by binding to basic regions of the RNA methyltransferase. Our findings further indicate that in BCS, nuclear disassembly of the import complex and release of EMG1(D86G) lead to its nuclear aggregation and degradation, resulting in the reduced nucleolar recruitment of the RNA methyltransferase and defects in the biogenesis of the small ribosomal subunit."],["dc.identifier.doi","10.1093/hmg/ddw351"],["dc.identifier.isi","000397063900007"],["dc.identifier.pmid","27798105"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38697"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/6"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P08: Kernporenpassage großer, makromolekularer Komplexe, wie beispielsweise ribosomaler Untereinheiten"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.issn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Görlich (Cellular Logistics)"],["dc.title","Effects of the Bowen-Conradi syndrome mutation in EMG1 on its nuclear import, stability and nucleolar recruitment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]