A Novel Adenosine Triphosphatase Isolated from RNA Polymerase Preparations of Escherichia coli: II. Enzymatic Properties and Molecular Structure1

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Abstract
An adenosinetriphosphatase (ATPase) [EC 3.6.1. 3] copurified with the DNA-dependent RNA polymerase [EC 2.7.7.6] from Escherichia coli was isolated to apparent homogeneity and some of its functional as well as structural properties were examined. Although the novel ATPase exhibited metal requirements similar to those of Mg2+, Ca2+-ATPase, its response to NaN2 and antisera appeared completely different from that of the Mg2+, Ca2+-ATPase. The purified ATPase was found to be a large protein with a molecular weight of 9.3×l105 daltons, composed of identical subunits of 7×104 daltons. When viewed under an electron microscope, the ATPase appeared to be very similar to material previously misidentified as the RNA polymerase. The physiological role of the novel ATPase, however, remains unclear.

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