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(Received for publication, March 5, 1996; and in revised form, March 18, 1996) A mutant of Escherichia coli lacking
phosphatidylethanolamine (PE) and a monoclonal antibody (mAb 4B1)
directed against a conformationally sensitive epitope (4B1) of lactose
permease were used to establish a novel role for a phospholipid in the
assembly of a membrane protein. Epitope 4B1 is readily detectable in
spheroplasts and right-side-out membrane vesicles from PE-containing
but not from PE-deficient cells expressing lactose permease. Lactose
permease from PE-containing membranes, but not from PE-deficient
membranes, subjected to sodium dodecyl sulfate (SDS)-polyacrylamide gel
electrophoresis and Western blot analysis is also recognized by mAb
4B1. If total E. coli phospholipids or PE (but not
phosphatidylcholine, phosphatidylglycerol, or cardiolipin) are blotted
on nitrocellulose sheets (Eastern blot) prior to transfer of proteins
from SDS-polyacrylamide gels, the permease from PE-deficient cells
regains its recognition by mAb 4B1. Therefore, PE is required during
assembly to form epitope 4B1, but, once formed, sufficient
``conformational memory'' is retained in the permease to
either retain or reform this epitope in the absence of PE. Lactose
permease lacking epitope 4B1 can be induced to form the epitope if
partially denatured and then renatured in the presence of PE
specifically. These results establish for the first time a role for PE
as a molecular chaperone in the assembly of the lactose permease.
Volume 271,
Number 20,
Issue of May 17, 1996 pp. 11615-11618
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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