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J Biol Chem, Vol. 273, Issue 46, 30139-30146, November 13, 1998
From the Division of Reproductive Biology, Department of Gynecology
and Obstetrics, Stanford University Medical School,
Stanford, California 94305-5317
Bok (Bcl-2-related
ovarian killer) is a proapoptotic Bcl-2 family
protein identified in the ovary based on its dimerization with the
antiapoptotic protein Mcl-1. In addition to the Bcl-2 homology (BH)
domains 1 and 2 and the transmembrane sequence, Bok also has a BH3
domain believed to be important for dimerization with selective
antiapoptotic Bcl-2 proteins and cell killing. We identified a splicing
variant of Bok mRNA with a deletion of 43 residues from the
full-length protein (Bok-L), leading to the fusion of the
N-terminal-half of its BH3 domain to the C-terminal-half of the BH1
domain. Genomic analysis indicated that the Bok has five exons, and the
short form of Bok (Bok-S) represents the splicing out of exon three
during transcription. Although Bok-S retains the apoptosis-inducing
activity in transfected cells, it has lost the ability to dimerize with
antiapoptotic proteins in vitro. Additional BH3 domain
mutations of Bok-L also led to defective heterodimerization without
affecting its proapoptotic action. Furthermore, similar deletions for
the related channel-forming proapoptotic Bax and Bak did not impair
their cell killing ability. Thus, the naturally occurring Bok-S variant
represents a new form of proapoptotic protein that induces cell killing
without heterodimerization with antiapoptotic Bcl-2 proteins. This
variant appears to contain the minimal module spanning BH1 and BH2
domains and the transmembrane sequence for apoptosis induction by
channel-forming Bcl-2 proteins.
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