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. 1987 Sep;169(9):4342–4348. doi: 10.1128/jb.169.9.4342-4348.1987

High-affinity potassium uptake system in Bacillus acidocaldarius showing immunological cross-reactivity with the Kdp system from Escherichia coli.

E P Bakker, A Borchard, M Michels, K Altendorf, A Siebers
PMCID: PMC213750  PMID: 2957359

Abstract

During growth with low levels of K+, Bacillus acidocaldarius expressed a high-affinity K+ uptake system. The following observations indicate that this system strongly resembles the Kdp-ATPase of Escherichia coli: (i) its high affinity for K+ (Km of 20 microM or below); (ii) its poor transport of Rb+; (iii) the enhanced ATPase activity of membranes derived from cells grown with low levels of K+ (this activity was stimulated by K+ and inhibited by vanadate); (iv) the expression of an extra protein with a molecular weight of 70,000 in cells grown with low levels of K+; and (v) the immunological cross-reactivity of this 70,000-molecular-weight protein with antibodies against the catalytic subunit B of the E. coli Kdp system. Antibodies against the complete E. coli Kdp system, which immunoprecipitated the whole E. coli KdpABC complex, almost exclusively precipitated the 70,000-molecular-weight protein from detergent-solubilized B. acidocaldarius membranes. The possibility that the B. acidocaldarius Kdp system consists of a single, KdpB-type subunit is discussed.

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Selected References

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