title: Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1.
abstract: The human TCF11 gene encodes a ubiquitously expressed bZIP transcription factor of the cap n' collar (CNC) domain family. It has a high sequence similarity to the erythroid-specific bZIP factor p45 NF-E2 in the CNC domain, which is involved in DNA binding. LCR-F1, a TCF11 isoform, is a more potent transcriptional activator than p45 NF-E2 in erythroid cells. We show here that the TCF11 protein interacts to form heterodimers with small Maf proteins, previously shown to dimerize with p45 NF-E2, ECH and Fos. Such heterodimerization significantly alters the DNA binding characteristics of TCF11. While TCF11 alone binds in vitro to the tandem NF-E2 site derived from 5' DNase hypersensitive site 2 in the beta-globin locus control region and to the single NF-E2 site in the porphobilinogen deaminase gene promoter, stronger binding is detected in the presence of small Maf proteins. Using antibodies, TCF11 isoforms bound to the single NF-E2 site were detected in K562 erythroid cell nuclear extracts. These findings place TCF11 as a good candidate for the proposed widely expressed factor(s) known to interact with small Maf proteins and bind NF-E2 sites in a sequence-specific manner resembling NF-E2.
authors.affiliation: Biotechnology Centre of Oslo, University of Oslo, Norway.
authors.forename: O
authors.initials: O
authors.lastname: Johnsen
authors.forename: N
authors.initials: N
authors.lastname: Skammelsrud
authors.forename: L
authors.initials: L
authors.lastname: Luna
authors.forename: M
authors.initials: M
authors.lastname: Nishizawa
authors.forename: H
authors.initials: H
authors.lastname: Prydz
authors.forename: A B
authors.initials: AB
authors.lastname: Kolstø
mesh_terms: D030161:Avian Proteins; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D050981:Erythroid-Specific DNA-Binding Factors; D006801:Humans; D011163:Hydroxymethylbilane Synthase / Q000235:genetics; D007118:Immunoassay; D016350:Leucine Zippers; D051258:MafB Transcription Factor; D051260:MafF Transcription Factor; D050983:NF-E2 Transcription Factor; D050984:NF-E2 Transcription Factor, p45 Subunit; D051265:NF-E2-Related Factor 1; D009687:Nuclear Proteins / Q000378:metabolism; D051266:Nuclear Respiratory Factor 1; D051264:Nuclear Respiratory Factors; D015513:Oncogene Proteins / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D051257:Proto-Oncogene Proteins c-maf; D015534:Trans-Activators / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*
chemical_list: D030161:Avian Proteins; D004268:DNA-Binding Proteins; D050981:Erythroid-Specific DNA-Binding Factors; C495607:MAF protein, human; C490407:MAFB protein, human; C082866:MAFF protein, Gallus gallus; C484147:MAFF protein, human; D051258:MafB Transcription Factor; D051260:MafF Transcription Factor; D050983:NF-E2 Transcription Factor; D050984:NF-E2 Transcription Factor, p45 Subunit; D051265:NF-E2-Related Factor 1; C494692:NFE2 protein, human; C088357:NFE2L1 protein, human; C495633:NRF1 protein, human; D009687:Nuclear Proteins; D051266:Nuclear Respiratory Factor 1; D051264:Nuclear Respiratory Factors; D015513:Oncogene Proteins; D011518:Proto-Oncogene Proteins; D051257:Proto-Oncogene Proteins c-maf; D015534:Trans-Activators; D014157:Transcription Factors; D004247:DNA; D011163:Hydroxymethylbilane Synthase