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Article: Structural Analysis of the Recognition of the Negative Regulator NmrA and DNA by the Zinc Finger from the GATA-Type Transcription Factor AreA

TitleStructural Analysis of the Recognition of the Negative Regulator NmrA and DNA by the Zinc Finger from the GATA-Type Transcription Factor AreA
Authors
Issue Date2008
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2008, v. 381 n. 2, p. 373-382 How to Cite?
AbstractAmongst the most common protein motifs in eukaryotes are zinc fingers (ZFs), which, although largely known as DNA binding modules, also can have additional important regulatory roles in forming protein:protein interactions. AreA is a transcriptional activator central to nitrogen metabolism in Aspergillus nidulans. AreA contains a GATA-type ZF that has a competing dual recognition function, binding either DNA or the negative regulator NmrA. We report the crystal structures of three AreA ZF-NmrA complexes including two with bound NAD + or NADP +. The molecular recognition of AreA ZF-NmrA involves binding of the ZF to NmrA via hydrophobic and hydrogen bonding interactions through helices α1, α6 and α11. Comparison with an earlier NMR solution structure of AreA ZF-DNA complex by overlap of the AreA ZFs shows that parts of helices α6 and α11 of NmrA are positioned close to the GATA motif of the DNA, mimicking the major groove of DNA. The extensive overlap of DNA with NmrA explains their mutually exclusive binding to the AreA ZF. The presence of bound NAD +/NADP + in the NmrA-AreaA ZF complex, however, causes minimal structural changes. Thus, any regulatory effects on AreA function mediated by the binding of oxidised nicotinamide dinucleotides to NmrA in the NmrA-AreA ZF complex appear not to be modulated via protein conformational rearrangements. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/171769
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKotaka, Men_US
dc.contributor.authorJohnson, Cen_US
dc.contributor.authorLamb, HKen_US
dc.contributor.authorHawkins, ARen_US
dc.contributor.authorRen, Jen_US
dc.contributor.authorStammers, DKen_US
dc.date.accessioned2012-10-30T06:16:55Z-
dc.date.available2012-10-30T06:16:55Z-
dc.date.issued2008en_US
dc.identifier.citationJournal Of Molecular Biology, 2008, v. 381 n. 2, p. 373-382en_US
dc.identifier.issn0022-2836en_US
dc.identifier.urihttp://hdl.handle.net/10722/171769-
dc.description.abstractAmongst the most common protein motifs in eukaryotes are zinc fingers (ZFs), which, although largely known as DNA binding modules, also can have additional important regulatory roles in forming protein:protein interactions. AreA is a transcriptional activator central to nitrogen metabolism in Aspergillus nidulans. AreA contains a GATA-type ZF that has a competing dual recognition function, binding either DNA or the negative regulator NmrA. We report the crystal structures of three AreA ZF-NmrA complexes including two with bound NAD + or NADP +. The molecular recognition of AreA ZF-NmrA involves binding of the ZF to NmrA via hydrophobic and hydrogen bonding interactions through helices α1, α6 and α11. Comparison with an earlier NMR solution structure of AreA ZF-DNA complex by overlap of the AreA ZFs shows that parts of helices α6 and α11 of NmrA are positioned close to the GATA motif of the DNA, mimicking the major groove of DNA. The extensive overlap of DNA with NmrA explains their mutually exclusive binding to the AreA ZF. The presence of bound NAD +/NADP + in the NmrA-AreaA ZF complex, however, causes minimal structural changes. Thus, any regulatory effects on AreA function mediated by the binding of oxidised nicotinamide dinucleotides to NmrA in the NmrA-AreA ZF complex appear not to be modulated via protein conformational rearrangements. © 2008 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_US
dc.relation.ispartofJournal of Molecular Biologyen_US
dc.subject.meshAspergillus Nidulans - Genetics - Metabolismen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshDna, Fungal - Genetics - Metabolismen_US
dc.subject.meshFungal Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNad - Chemistry - Metabolismen_US
dc.subject.meshNadp - Chemistry - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRepressor Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshTranscription Factors - Chemistry - Metabolismen_US
dc.subject.meshTranscription, Geneticen_US
dc.subject.meshZinc Fingersen_US
dc.titleStructural Analysis of the Recognition of the Negative Regulator NmrA and DNA by the Zinc Finger from the GATA-Type Transcription Factor AreAen_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.jmb.2008.05.077en_US
dc.identifier.pmid18602114-
dc.identifier.scopuseid_2-s2.0-47049121925en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-47049121925&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume381en_US
dc.identifier.issue2en_US
dc.identifier.spage373en_US
dc.identifier.epage382en_US
dc.identifier.isiWOS:000258483600012-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.f10001119373-
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridJohnson, C=7405664788en_US
dc.identifier.scopusauthoridLamb, HK=7103263399en_US
dc.identifier.scopusauthoridHawkins, AR=7102975292en_US
dc.identifier.scopusauthoridRen, J=7403083572en_US
dc.identifier.scopusauthoridStammers, DK=34573122600en_US

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