Abstract
A novel human member of the Bcl-2 family was identified, Bcl-B, which is closest in amino acid sequence homology to the Boo (Diva) protein. The Bcl-B protein contains four Bcl-2 homology (BH) domains (BH1, BH2, BH3, BH4) and a predicted carboxyl-terminal transmembrane (TM) domain. The BCL-B mRNA is widely expressed in adult human tissues. The Bcl-B protein binds Bcl-2, Bcl-X(L), and Bax but not Bak. In transient transfection assays, Bcl-B suppresses apoptosis induced by Bax but not Bak. Deletion of the TM domain of Bcl-B impairs its association with intracellular organelles and diminishes its anti-apoptotic function. Bcl-B thus displays a unique pattern of selectivity for binding and regulating the function of other members of the Bcl-2 family.
Highlights
A novel human member of the Bcl-2 family was identified, Bcl-2 family protein resembling Boo” (Bcl-B), which is closest in amino acid sequence homology to the Boo (Diva) protein
We describe a new member of the human Bcl-2 family protein, Bcl-B
One report has suggested that the Boo protein can bind Bak but not Bax, and provided evidence that Boo suppresses apoptosis induced by overexpression of Bak but not Bax [10]
Summary
A novel human member of the Bcl-2 family was identified, Bcl-B, which is closest in amino acid sequence homology to the Boo (Diva) protein. Bcl-2 family proteins contain at least one of four conserved regions, termed Bcl-2 homology (BH) domains. Most members of this family contain a TM domain located near their carboxyl terminus that anchors them in intracellular membranes of mitochondria and other organelles Tion partners and tissue-specific patterns of expression combine to endow each mammalian Bcl-2 family protein with a unique physiological role in vivo, resulting for example in highly diverse phenotypes when members of this multigene family are individually knocked out in mice (reviewed in Ref. 4). We describe the molecular cloning and initial characterization of a new human member of the Bcl-2 family, Bcl-B
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