Nucleic Acids Research, Vol 25, Issue 15 2953-2959, Copyright © 1997 by Oxford University Press
H Motohashi, JA Shavit, K Igarashi, M Yamamoto and JD Engel
Maf family proteins are so named because of their structural similarity to
the founding member, the oncoprotein v-Maf. The small Maf proteins (MafF,
MafG and MafK), as do all family members, include a characteristic basic
region linked to a leucine zipper (b-Zip) domain which mediate DNA binding
and subunit dimerization respectively. The small Maf proteins form
homodimers or heterodimers with other b-Zip proteins present in the cell
and bind to Maf recognition elements (MARE) in DNA. Since they lack known
transcriptional activation domains, the small Maf proteins function either
as obligatory heterodimeric partner molecules with numerous large subunits,
discussed below, or alternatively as homo- or heterodimeric transcriptional
repressors. The three small Maf proteins are expressed in a number of
overlapping tissues, but their expression profiles nonetheless appear to be
under meticulous tissue- and developmental stage-specific control. The MARE
bears a striking resemblance to the NF-E2 binding sequence. NF-E2 binding
sites in the human beta-globin locus control region have been directly
implicated as integral components in the circuitry required for eliciting
changes in chromatin structure that precede globin gene activation. While
the NF-E2 DNA sequence has been shown to be important for
erythroid-specific gene regulation, a growing list of other genes may also
be regulated through the same, or very similar, cis elements in
non-erythroid cells. Taken together, these observations argue that
comprehensive analysis of the activities of the small Maf proteins may
provide a unique perspective for expanding our understanding of
transcriptional regulation that can be elicited through interacting
transcription factor networks.
REVIEWS
The world according to Maf
Institute of Basic Medical Sciences and Center for TARA, University of Tsukuba, Tsukuba 305, Japan.
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