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J. Biol. Chem., Vol. 266, Issue 24, 16157-16164, 08, 1991
B Vilsen, JP Andersen and DH MacLennan
Site-specific mutagenesis of the sarcoplasmic reticulum Ca(2+)-ATPase was
used to investigate the functional roles of 18 amino acid residues located
at or near the "hinge-domain," a highly conserved region of the
cation-transporting ATPases. Mutation of Lys684 to arginine, alanine,
histidine, and glutamine resulted in complete loss of calcium transport
function and ATPase activity. For the Lys684----Ala, histidine, and
glutamine mutants, this coincided with a loss of the ability to form a
phosphorylated intermediate from ATP or Pi. The Lys684----Arg mutant
retained the ability to phorphorylate from ATP with normal apparent
affinity, demonstrating the importance of the positive charge. On the other
hand, no phosphorylation was observed with Pi as substrate in this mutant.
Examination of the partial reactions after phosphorylation from ATP in the
Lys684----Arg mutant demonstrated a reduction of the rate of transformation
of the ADP-sensitive phosphoenzyme intermediate (E1P) to the
ADP-insensitive phosphoenzyme intermediate (E2P), which could account for
the loss of transport function. Once accumulated, the E2P intermediate was
able to decompose rapidly in the presence of K+ at neutral pH. These
results may be interpreted in terms of a preferential destabilization of
protein phosphate interactions in the E2P form of this mutant. The
Asp703----Ala and Asn-Asp707----Ala-Ala mutants were completely inactive
and unable to form phosphoenzyme intermediates from ATP or Pi. In these
mutants as well as in the Lys684----Ala mutant, nucleotides were found to
protect with normal affinity against intramolecular cross-linking induced
with glutaraldehyde, indicating that the nucleotide binding site was
intact. Mutation of Glu646, Glu647, Asp659, Asp660, Glu689, Asp695, Glu696,
Glu715, and Glu732 to alanine did not affect the maximum rates of calcium
transport and ATP hydrolysis or the apparent affinities for calcium and
ATP. Mutation of the 2 highly conserved proline residues, Pro681 and
Pro709, as well as Lys728, to alanine resulted in partially inhibited
Ca(2+)-ATPase enzymes with retention of the ability to form a phosphoenzyme
intermediate from ATP or Pi and with normal apparent affinities for ATP and
calcium. The proline mutants retained the biphasic ATP concentration
dependence of ATPase activity, characteristic of the wild- type, and
therefore the partial inhibition of turnover could not be ascribed to a
disruption of the low affinity modulatory ATP site.(ABSTRACT TRUNCATED AT
400 WORDS)
Functional consequences of alterations to amino acids located in the hinge domain of the Ca(2+)-ATPase of sarcoplasmic reticulum
Danish Biomembrane Research Centre, Institute of Physiology, University of Aarhus.
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