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Title
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RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel family of homodimeric and heterodimeric DNA-binding proteins.
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Authors
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W.Reith,
C.Ucla,
E.Barras,
A.Gaud,
B.Durand,
C.Herrero-Sanchez,
M.Kobr,
B.Mach.
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Ref.
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Mol Cell Biol, 1994,
14,
1230-1244.
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PubMed id
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Abstract
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RFX1 is a transactivator of human hepatitis B virus enhancer I. We show here
that RFX1 belongs to a previously unidentified family of DNA-binding proteins of
which we have cloned three members, RFX1, RFX2, and RFX3, from humans and mice.
Members of the RFX family constitute the nuclear complexes that have been
referred to previously as enhancer factor C, EP, methylation-dependent
DNA-binding protein, or rpL30 alpha. RFX proteins share five strongly conserved
regions which include the two domains required for DNA binding and dimerization.
They have very similar DNA-binding specificities and heterodimerize both in
vitro and in vivo. mRNA levels for all three genes, particularly RFX2, are
elevated in testis. In other cell lines and tissues, RFX mRNA levels are
variable, particularly for RFX2 and RFX3. RFX proteins share several novel
features, including new DNA-binding and dimerization motifs and a peculiar
dependence on methylated CpG dinucleotides at certain sites.
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