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J Biol Chem, Vol. 273, Issue 43, 28430-28437, October 23, 1998
From the Medical Research Council Group in Membrane Biology,
Departments of Medicine and Biochemistry, University of Toronto,
Toronto M5S 1A8, Canada
In this study, we provide evidence that the
33-residue carboxyl-terminal (Ct) region of the human erythrocyte
chloride/bicarbonate exchanger, band 3, binds carbonic anhydrase II
(CAII). Immunofluorescence showed that tomato lectin-mediated
clustering of band 3 in ghost membranes caused a similar clustering of
CAII, indicating an in situ association. CAII cosolubilized
and coimmunoprecipitated with band 3, suggesting that the two proteins
form a complex. Band 3 (K1/2 = 70 nM) or the membrane domain of band 3 (K1/2 = 100 nM) bound saturably to
immobilized CAII in a solid phase binding assay. The interaction with
CAII was specifically blocked by an antibody to the Ct of band 3. Affinity blotting showed that a glutathione S-transferase
(GST)-fusion protein (GST-Ct) containing the last 33 residues of human
band 3 bound to CAII. The solid phase binding assay showed that binding
of GST-Ct to immobilized CAII was saturable
(K1/2 = 20 nM). The binding rate
was slow (t1/2 = 12 h) at physiological
ionic strength and pH but was enhanced at low ionic strength or acidic
pH. Intact band 3 (Ki = 15 nM), the
membrane domain of band 3 (Ki = 100 nM), or antibodies to the Ct of band 3 were able to block
GST-Ct binding to CAII, confirming the specificity of the interaction.
Affinity chromatography showed that CAII bound to immobilized GST-Ct
with a 1:1 stoichiometry. This work indicates that CAII, the
bicarbonate supplier, is directly coupled to band 3, the
chloride/bicarbonate exchanger in red blood cells.
Carbonic Anhydrase II Binds to the Carboxyl Terminus of Human
Band 3, the Erythrocyte
Cl
/HCO3
Exchanger
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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