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(Received for publication, November 7, 1995; and in revised form, February 15, 1996) Bcl-2 and Bax are members of a family of cytoplasmic proteins
that regulate apoptosis. The two proteins have highly similar amino
acid sequences but are functionally opposed: Bcl-2 acts to inhibit
apoptosis, whereas Bax counteracts this effect. The antagonism appears
to depend upon dimerization between Bcl-2 and Bax, but its mechanism is
otherwise unknown. Here we report that overexpressing Bax induces
apoptosis in a mammalian fibroblast cell line, and we identify a novel,
short ``suicide domain'' in Bax that is required for this
effect. Inserting this domain in place of the corresponding, divergent
sequence in Bcl-2 converts Bcl-2 from an inhibitor into an activator of
cell death. These findings imply that a specific region in Bax confers
an active propensity for apoptosis in mammalian cells and support the
view that Bcl-2 may block death primarily by suppressing Bax activity.
Volume 271,
Number 15,
Issue of April 12, 1996 pp. 8521-8524
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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