Nucleic Acids Research, Vol 25, Issue 4 843-849, Copyright © 1997 by Oxford University Press
JL Kalenik, D Chen, ME Bradley, SJ Chen and TC Lee
Muscle-restricted transcription of sarcomeric actin genes is negatively
controlled by the zinc finger protein YY1, which is down-regulated at the
protein level during myogenic differentiation. To identify cellular
proteins that might mediate the function/stability of YY1 in muscle cells,
we screened an adult human muscle cDNA library using the yeast two-hybrid
cloning system. We report the isolation and characterization of a novel
protein termed YAF2 (YY1- associated factor 2) that interacts with YY1. The
YAF2 cDNA encodes a 180 amino acid basic protein (pI 10.5) containing a
single N-terminal C2-X10-C2 zinc finger. Lysine clusters are present that
may function as a nuclear localization signal. Domain mapping analysis
shows that the first and second zinc fingers of YY1 are targeted for YAF2
protein interaction. In contrast to the down-regulation of YY1, YAF2
message levels increase during in vitro differentiation of both rat
skeletal and cardiac muscle cells. YAF2 appears to have a promyogenic
regulatory role, since overexpression of YAF2 in C2 myoblasts stimulates
myogenic promoter activity normally restricted by YY1. Co-transfection of
YY1 reverses the stimulatory effect of YAF2. YAF2 also greatly potentiates
proteolytic cleavage of YY1 by the calcium- activated protease m- calpain.
The isolation of YAF2 may help in understanding the mechanisms through
which inhibitors of myogenic transcription may be antagonized or eliminated
by proteolysis during muscle development.
ARTICLES
Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1
Department of Biochemistry, SUNY at Buffalo, NY 14214, USA.
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