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Volume 271, Number 38, Issue of September 20, 1996 pp. 22983-22989
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Functional and Physical Interactions between Partial Molecules of STE6, a Yeast ATP-binding Cassette Protein

(Received for publication, April 9, 1996, and in revised form, July 5, 1996)

From the Department of Cell Biology and Anatomy, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205

The Saccharomyces cerevisiae a-factor transporter, STE6, is a member of the ATP binding cassette (ABC) transporter superfamily. ABC proteins consist of four modular units that comprise two membrane-spanning domains (MSDs) and two nucleotide-binding domains (NBDs). Like many ABC proteins, STE6 contains these four domains in a single polypeptide; certain other ABC proteins are encoded as pairs of ``half-molecules'' or are further subdivided. Our previous studies demonstrated that STE6 can be expressed as two half-molecules that are functional when co-expressed. Here we dissect the interactions between modules of STE6 in greater detail. We show by co-immunoprecipitation that STE6 half-molecules interact physically, supporting the view that they co-assemble in vivo to form a functional transporter. We also demonstrate a physical interaction between a STE6 half-molecule and full-length STE6; such complexes appear to be functional, based on the striking finding that the defective activity of full-length STE6 mutated in one of its NBDs can be corrected by co-expression of the corresponding ``wild-type'' half-molecule. We also show that a quarter-molecule consisting solely of the N-terminal MSD of STE6 can interact physically and functionally with a C-terminal three-quarter molecule of STE6, indicating that information directing the assembly of STE6 from partial molecules is contained, at least in part, within its membrane spans.

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