Nucleic Acids Research, Vol 24, Issue 21 4289-4297, Copyright © 1996 by Oxford University Press
O Johnsen, N Skammelsrud, L Luna, M Nishizawa, H Prydz and AB Kolsto
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.
ARTICLES
Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1
Biotechnology Centre of Oslo, University of Oslo, Norway.
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