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The in vitro insertion of monoamine oxidase B into mitochondrial outer membranes
Author(s) -
Zhuang Z.,
Hogan M.,
McCauley R.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80253-9
Subject(s) - monoamine oxidase , in vitro , membrane , chemistry , mitochondrion , biochemistry , microbiology and biotechnology , biophysics , biology , enzyme
Bovine monoamine oxidase (MAO) B has been synthesized in vitro using a reticulocyte lysate translation system directed by bovine liver poly(A) + RNA. The newly synthesized enzyme apparently lacks a cleavable N‐terminal extension, but MAO B is readily incorporated into mitochondria or isolated mitochondrial outer membranes prepared from rat liver. ATP is not required for the binding of the newly synthesized enzyme to the outer membranes, but is necessary for the insertion of MAO B into these membrane vesicles. The ATP is not required to generate a mitochondrial membrane potential as assembly occurs under conditions that preclude either the formation or the maintenance of the potential. MAO B will bind to but not become incorporated into outer membrane vesicles which have been treated with trypsin, suggesting that the insertion of MAO B also depends on protein factors present on the outer membranes.