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dc.contributor.authorBjørnstad, Linn
dc.contributor.authorMeza, Trine Johansen
dc.contributor.authorOtterlei, Marit
dc.contributor.authorOlafsrud, Solveig Mjelstad
dc.contributor.authorMeza-Zepeda, Leonardo Andrés
dc.contributor.authorFalnes, Pål
dc.date.accessioned2015-11-10T12:50:16Z
dc.date.accessioned2015-11-24T09:06:39Z
dc.date.available2015-11-10T12:50:16Z
dc.date.available2015-11-24T09:06:39Z
dc.date.issued2012
dc.identifier.citationPLoS ONE 2012, 7(11)nb_NO
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11250/2365387
dc.description.abstractThe Fe(II)- and 2-oxoglutarate (2OG)-dependent dioxygenase AlkB from E. coli is a demethylase which repairs alkyl lesions in DNA, as well as RNA, through a direct reversal mechanism. Humans possess nine AlkB homologs (ALKBH1-8 and FTO). ALKBH2 and ALKBH3 display demethylase activities corresponding to that of AlkB, and both ALKBH8 and FTO are RNA modification enzymes. The biochemical functions of the rest of the homologs are still unknown. To increase our knowledge on the functions of ALKBH4 and ALKBH7 we have here performed yeast two-hybrid screens to identify interaction partners of the two proteins. While no high-confidence hits were detected in the case of ALKBH7, several proteins associated with chromatin and/or involved in transcription were found to interact with ALKBH4. For all interaction partners, the regions mediating binding to ALKBH4 comprised domains previously reported to be involved in interaction with DNA or chromatin. Furthermore, some of these partners showed nuclear co-localization with ALKBH4. However, the global gene expression pattern was only marginally altered upon ALKBH4 over-expression, and larger effects were observed in the case of ALKBH7. Although the molecular function of both proteins remains to be revealed, our findings suggest a role for ALKBH4 in regulation of gene expression or chromatin state.nb_NO
dc.language.isoengnb_NO
dc.publisherPublic Library of Sciencenb_NO
dc.titleHuman ALKBH4 Interacts with Proteins Associated with Transcriptionnb_NO
dc.typeJournal articlenb_NO
dc.typePeer revieweden_GB
dc.date.updated2015-11-10T12:50:16Z
dc.source.volume7nb_NO
dc.source.journalPLoS ONEnb_NO
dc.source.issue11nb_NO
dc.identifier.doi10.1371/journal.pone.0049045
dc.identifier.cristin988715
dc.description.localcode© 2012 Bjørnstad et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.nb_NO


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