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J. Biol. Chem., Vol. 265, Issue 9, 4929-4933, 03, 1990
Z Chen-Levy and ML Cleary
The Bcl-2 oncogenic protein was synthesized in vitro and shown to post-
translationally integrate asymmetrically into microsomal membranes with no
requirement for an amino-terminal signal sequence. Instead, a
carboxyl-terminal hydrophobic domain of Bcl-2 served as an insertion
sequence essential for membrane assembly since a Bcl-2 mutant lacking this
domain completely lost its ability to associate with microsomal membranes.
The data demonstrate that Bcl-2 is tightly associated with the lipid
bilayer with the nature of an integral membrane protein. The membrane
orientation of Bcl-2 was determined using a protease protection assay,
which showed that it is predominantly localized to the cytoplasmic face of
membranes. A similar type of membrane processing has been shown for
cytochrome b5 and also suggested for the viral oncogenic protein polyoma
middle-T antigen.
Membrane topology of the Bcl-2 proto-oncogenic protein demonstrated in vitro
Department of Pathology, Stanford University School of Medicine, California 94305.
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