Small Maf Proteins Interact With the Human Transcription Factor TCF11/Nrf1/LCR-F1

Authors: Johnsen, Øyvind; Prydz, Hans

Source: Nucleic Acids Research, Volume 24, Number 21, November 1996 , pp. 4289-4297(9)

Publisher: Oxford University Press

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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 vitroto the tandem NF-E2 site derived from 5′ DNase hypersensitive site 2 in the ß-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.

Document Type: Research article

Publication date: 1996-11-01

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