2.50
HDL Handle:
http://hdl.handle.net/10033/225931
Title:
Mapping of NRF binding motifs of NF-kappaB p65 subunit.
Authors:
Reboll, Marc R; Schweda, Aike T; Bartels, Myriam; Franke, Raimo; Frank, Ronald; Nourbakhsh, Mahtab
Abstract:
NF-kappaB repressing factor (NRF) is a nuclear transcription factor that binds to a specific DNA sequence in NF-kappaB target promoters. Previous reports suggested that NRF interferes with the transcriptional activity of NF-kappaB binding sites through a direct interaction with NF-kappaB subunits. The aim of this study was to map specific NRF binding domains in the NF-kappaB proteins, p65 and p50. Our data demonstrate that NRF is able to interact with the p65 subunit and inhibit its transcription enhancing activity in reporter gene experiments. Using tandem affinity purifications (TAP), we show that NRF protein significantly binds to the endogenous p65, subunit but not to the p50 subunit. The selective binding activity of the NRF protein is consistently mediated by the N-terminal domain of NRF (Amino acids 1-380). Moreover, the Rel homology domain (RHD) of p65 is sufficient for binding to the N-terminal domain of NRF. Using detailed peptide mapping studies, we finally identify three peptide motifs in p65 RHD showing distinctive binding specificities for the NRF protein. According to the predicted structure of p65, all three peptide motifs align within an exposed region of p65 and might hint at promising targets for inhibitors.
Affiliation:
Department of Chemical Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
Citation:
Mapping of NRF binding motifs of NF-kappaB p65 subunit. 2011, 150 (5):553-62 J. Biochem.
Journal:
Journal of biochemistry
Issue Date:
Nov-2011
URI:
http://hdl.handle.net/10033/225931
DOI:
10.1093/jb/mvr099
PubMed ID:
21821668
Type:
Article
Language:
en
ISSN:
1756-2651
Appears in Collections:
Publications of Dept. Chemical Biology (CBIO)

Full metadata record

DC FieldValueLanguage
dc.contributor.authorReboll, Marc Ren_GB
dc.contributor.authorSchweda, Aike Ten_GB
dc.contributor.authorBartels, Myriamen_GB
dc.contributor.authorFranke, Raimoen_GB
dc.contributor.authorFrank, Ronalden_GB
dc.contributor.authorNourbakhsh, Mahtaben_GB
dc.date.accessioned2012-05-25T08:40:07Z-
dc.date.available2012-05-25T08:40:07Z-
dc.date.issued2011-11-
dc.identifier.citationMapping of NRF binding motifs of NF-kappaB p65 subunit. 2011, 150 (5):553-62 J. Biochem.en_GB
dc.identifier.issn1756-2651-
dc.identifier.pmid21821668-
dc.identifier.doi10.1093/jb/mvr099-
dc.identifier.urihttp://hdl.handle.net/10033/225931-
dc.description.abstractNF-kappaB repressing factor (NRF) is a nuclear transcription factor that binds to a specific DNA sequence in NF-kappaB target promoters. Previous reports suggested that NRF interferes with the transcriptional activity of NF-kappaB binding sites through a direct interaction with NF-kappaB subunits. The aim of this study was to map specific NRF binding domains in the NF-kappaB proteins, p65 and p50. Our data demonstrate that NRF is able to interact with the p65 subunit and inhibit its transcription enhancing activity in reporter gene experiments. Using tandem affinity purifications (TAP), we show that NRF protein significantly binds to the endogenous p65, subunit but not to the p50 subunit. The selective binding activity of the NRF protein is consistently mediated by the N-terminal domain of NRF (Amino acids 1-380). Moreover, the Rel homology domain (RHD) of p65 is sufficient for binding to the N-terminal domain of NRF. Using detailed peptide mapping studies, we finally identify three peptide motifs in p65 RHD showing distinctive binding specificities for the NRF protein. According to the predicted structure of p65, all three peptide motifs align within an exposed region of p65 and might hint at promising targets for inhibitors.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Journal of biochemistryen_GB
dc.subject.meshAmino Acid Motifsen_GB
dc.subject.meshAmino Acid Sequenceen_GB
dc.subject.meshHeLa Cellsen_GB
dc.subject.meshHumansen_GB
dc.subject.meshMolecular Sequence Dataen_GB
dc.subject.meshProtein Bindingen_GB
dc.subject.meshRepressor Proteinsen_GB
dc.subject.meshTranscription Factor RelAen_GB
dc.titleMapping of NRF binding motifs of NF-kappaB p65 subunit.en
dc.typeArticleen
dc.contributor.departmentDepartment of Chemical Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany.en_GB
dc.identifier.journalJournal of biochemistryen_GB

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.