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J. Biol. Chem., Vol. 263, Issue 35, 18664-18668, Dec, 1988

The fluorescein isothiocyanate-binding site of the plasma-membrane H+- ATPase of Neurospora crassa

JP Pardo and CW Slayman
Department of Human Genetics, Yale University School of Medicine, New Haven, Connecticut 06510.

The mammalian (Na+,K+), Ca2+-, and (H+,K+)-ATPases contain a well- characterized lysine residue that reacts with fluorescein 5'- isothiocyanate (FITC); enzymatic activity is protected by ATP, suggesting that the residue is located in or near the nucleotide- binding domain. In this study, the plasma-membrane H+-ATPase of Neurospora crassa is also shown to be sensitive to FITC. The reaction occurs with pseudo first-order kinetics, has a pKa of 8.0, and is stimulated by Mg2+. Enzymatic activity is protected by MgADP with a Kd of 0.2-0.3 mM, close to the Ki with which MgADP serves as a competitive inhibitor of ATP hydrolysis. A tryptic peptide labeled with FITC in the absence, but not in the presence, of MgADP has been isolated and sequenced. The FITC-sensitive residue is Lys474, located in a region that exhibits significant homology with the mammalian cation- transporting ATPases.
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