منابع مشابه
Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli.
During ATP hydrolysis the K+-translocating Kdp-ATPase from Escherichia coli forms a phosphorylated intermediate as part of the catalytic cycle. The influence of effectors (K+, Na+, Mg2+, ATP, ADP) and inhibitors (vanadate, N-ethylmaleimide, bafilomycin A1) on the phosphointermediate level and on the ATPase activity was analyzed in purified wild-type enzyme (apparent Km = 10 microM) and a KdpA m...
متن کاملRapid, high yield purification and characterization of the K(+)-translocating Kdp-ATPase from Escherichia coli.
The conventional procedure for the purification of the high affinity K+ uptake ATPase (KdpABC) from Escherichia coli involves a tedious three-column protocol (final enzyme purity, approximately 90%; activity yield, 6.5% (Siebers, A., and Altendorf, K. (1988) Eur. J. Biochem. 178, 131-140)). We have now developed a highly effective one-column (Fractogel TSK AF-Red) protocol yielding an enzyme pr...
متن کاملThe products of the kdpDE operon are required for expression of the Kdp ATPase of Escherichia coli.
The expression of the Kdp system for K+ uptake in Escherichia coli requires the products of two genes, kdpD and kdpE. These genes constitute an operon adjacent to the kdpABC operon that encodes the three membrane protein subunits of Kdp. Both operons are transcribed in the same direction and overlap; the kdpDE promoter is in kdpC, the last gene of the kdpABC operon. Transcription of the kdpDE o...
متن کاملRotation of Escherichia coli F(1)-ATPase.
By applying the same method used for F(1)-ATPase (TF(1)) from thermophilic Bacillus PS3 (Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997) Nature 386, 299-302), we observed ATP-driven rotation of a fluorescent actin filament attached to the gamma subunit in Escherichia coli F(1)-ATPase. The torque value and the direction of the rotation were the same as those observed for TF(1). F...
متن کاملCs(+) induces the kdp operon of Escherichia coli by lowering the intracellular K(+) concentration.
Cs(+) was found to induce expression of the kdpFABC operon, encoding a high-affinity K(+) uptake system of Escherichia coli. Quantitative expression analyses at the transcriptional and translational levels reveal that CsCl causes much higher induction of kdpFABC than does NaCl. A decrease of the intracellular K(+) concentration is found in cells exposed to CsCl. The results indicate that kdpFAB...
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ژورنال
عنوان ژورنال: Annals of the New York Academy of Sciences
سال: 1992
ISSN: 0077-8923,1749-6632
DOI: 10.1111/j.1749-6632.1992.tb43799.x