Warda, Ahmed Samir

[["dc.bibliographiccitation.firstpage","2004"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","2014"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Warda, Ahmed S"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Sloan, Katherine E"],["dc.contributor.author","Bohnsack, Markus T"],["dc.date.accessioned","2020-12-10T18:42:38Z"],["dc.date.available","2020-12-10T18:42:38Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.15252/embr.201744940"],["dc.identifier.eissn","1469-3178"],["dc.identifier.issn","1469-221X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78032"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Human METTL16 is a N 6 ‐methyladenosine (m 6 A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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","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"]]

[["dc.bibliographiccitation.firstpage","1138"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","1152"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Warda, Ahmed S."],["dc.contributor.author","Sharma, Sunny"],["dc.contributor.author","Entian, Karl-Dieter"],["dc.contributor.author","Lafontaine, Denis L. J."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:15:15Z"],["dc.date.available","2020-12-10T18:15:15Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1080/15476286.2016.1259781"],["dc.identifier.eissn","1555-8584"],["dc.identifier.issn","1547-6286"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16847"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74793"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Tuning the ribosome: The influence of rRNA modification on eukaryotic ribosome biogenesis and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2104"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","2119"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Ranjan, Namit"],["dc.contributor.author","Warda, Ahmed S."],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Blessing, Charlotte"],["dc.contributor.author","Hübner, Benedikt"],["dc.contributor.author","Seikowski, Jan"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:44:33Z"],["dc.date.available","2017-09-07T11:44:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Mitochondrial gene expression uses a non-universal genetic code in mammals. Besides reading the conventional AUG codon, mitochondrial (mt-)tRNA(Met) mediates incorporation of methionine on AUA and AUU codons during translation initiation and on AUA codons during elongation. We show that the RNA methyltransferase NSUN3 localises to mitochondria and interacts with mt-tRNA(Met) to methylate cytosine 34 (C34) at the wobble position. NSUN3 specifically recognises the anticodon stem loop (ASL) of the tRNA, explaining why a mutation that compromises ASL basepairing leads to disease. We further identify ALKBH1/ABH1 as the dioxygenase responsible for oxidising m(5)C34 of mt-tRNA(Met) to generate an f(5)C34 modification. In vitro codon recognition studies with mitochondrial translation factors reveal preferential utilisation of m(5)C34 mt-tRNA(Met) in initiation. Depletion of either NSUN3 or ABH1 strongly affects mitochondrial translation in human cells, implying that modifications generated by both enzymes are necessary for mt-tRNA(Met) function. Together, our data reveal how modifications in mt-tRNA(Met) are generated by the sequential action of NSUN3 and ABH1, allowing the single mitochondrial tRNA(Met) to recognise the different codons encoding methionine."],["dc.identifier.doi","10.15252/embj.201694885"],["dc.identifier.gro","3141604"],["dc.identifier.isi","000385707500006"],["dc.identifier.pmid","27497299"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/235"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/5"],["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","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation","SFB 1190 | P16: Co-translationaler Einbau von Proteinen in die bakterielle Plasmamembran"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Rodnina"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","NSUN3 and ABH1 modify the wobble position of mt-tRNA(Met) to expand codon recognition in mitochondrial translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]