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J Biol Chem, Vol. 273, Issue 18, 11075-11081, May 1, 1998

Regions of Association between the  and the  Subunit of the Gastric H,K-ATPase

Dominique Melle-Milovanovic, Marko Milovanovic, Sunil Nagpal, George Sachs, and Jai Moo Shin

From the Department of Medicine and Physiology, UCLA and Wadsworth Veterans Affairs Hospital, Los Angeles, California 90073 and  Allergan Pharmaceuticals, Irvine, California 92715

A binding and a yeast two-hybrid analysis were carried out on the gastric H,K-ATPase to determine interactive regions of the extracytoplasmic domains of the  and  subunits of this P type ATPase. Wheat germ agglutinin fractionation of fluorescein 5-maleimide-labeled tryptic fragments of detergent-solubilized H,K-ATPase showed that a fragment Leu⁸⁵⁵ to Arg⁹²² of the  subunit was bound to the  subunit. The yeast two-hybrid system showed that the region containing only a part of the seventh transmembrane segment, the loop, and part of the eighth transmembrane segment was capable of giving positive interaction signals with the ectodomain of the  subunit. The sequence in the extracytoplasmic loop close to the eighth transmembrane segment, namely Arg⁸⁹⁸ to Thr⁹²⁸, was identified as being the site of interaction using this method. We deduced that the sequence Arg⁸⁹⁸ to Arg⁹²² in the  subunit has strong interaction with the extracytoplasmic domain of the  subunit. Again, using yeast two-hybrid analysis, two different sequences in the  subunit Gln⁶⁴ to Asn¹³⁰ and Ala¹⁵⁶ to Arg¹⁸⁸ were identified as association domains in the extracytoplasmic sequence of the  subunit. These data enable identification of major associative regions of the - subunits of the H,K-ATPase.

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