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Vol. 8, Issue 10, 1901-1910, October 1997
The Molecular and Cell Biology Program, The University of Texas at
Dallas, Richardson, Texas 75083-0688
Coatomer is the soluble precursor of the COPI coat (coat protein I)
involved in traffic among membranes of the endoplasmic reticulum and
the Golgi apparatus. We report herein that neomycin precipitates
coatomer from cell extracts and from purified coatomer preparations.
Precipitation first increased and then decreased as the neomycin
concentration increased, analogous to the precipitation of a polyvalent
antigen by divalent antibodies. This suggested that neomycin
cross-linked coatomer into large aggregates and implies that coatomer
has two or more binding sites for neomycin. A variety of other
aminoglycoside antibiotics precipitated coatomer, or if they did not
precipitate, they interfered with the ability of neomycin to
precipitate. Coatomer is known to interact with a motif (KKXX)
containing adjacent lysine residues at the carboxyl terminus of the
cytoplasmic domains of some membrane proteins resident in the
endoplasmic reticulum. All of the antibiotics that interacted with
coatomer contain at least two close amino groups, suggesting that the
antibiotics might be interacting with the di-lysine binding site of
coatomer. Consistent with this idea, di-lysine itself blocked the
interaction of antibiotics with coatomer. Moreover, di-lysine and
antibiotics each blocked the coating of Golgi membranes by coatomer.
These data suggest that certain aminoglycoside antibiotics interact
with di-lysine binding sites on coatomer and that coatomer contains at
least two of these di-lysine binding sites.
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