2.50
Hdl Handle:
http://hdl.handle.net/10033/620824
Title:
Mapping of NRF binding motifs of NF-kappaB p65 subunit.
Authors:
Reboll, Marc R; Schweda, Aike T; Bartels, Myriam; Franke, Raimo; Frank, Ronald ( 0000-0003-2683-6511 ) ; 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:
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 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/10033/620824
DOI:
10.1093/jb/mvr099
PubMed ID:
21821668
Type:
Article
Language:
en
ISSN:
1756-2651
Appears in Collections:
Publications of the research group Chemical Biology (CBIO)

Full metadata record

DC FieldValue Language
dc.contributor.authorReboll, Marc Ren
dc.contributor.authorSchweda, Aike Ten
dc.contributor.authorBartels, Myriamen
dc.contributor.authorFranke, Raimoen
dc.contributor.authorFrank, Ronalden
dc.contributor.authorNourbakhsh, Mahtaben
dc.date.accessioned2017-02-16T14:58:35Z-
dc.date.available2017-02-16T14:58:35Z-
dc.date.issued2011-11-
dc.identifier.citationMapping of NRF binding motifs of NF-kappaB p65 subunit. 2011, 150 (5):553-62 J. Biochem.en
dc.identifier.issn1756-2651-
dc.identifier.pmid21821668-
dc.identifier.doi10.1093/jb/mvr099-
dc.identifier.urihttp://hdl.handle.net/10033/620824-
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
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAmino Acid Motifsen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshHeLa Cellsen
dc.subject.meshHumansen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshProtein Bindingen
dc.subject.meshRepressor Proteinsen
dc.subject.meshTranscription Factor RelAen
dc.titleMapping of NRF binding motifs of NF-kappaB p65 subunit.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalJournal of biochemistryen

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