A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure.

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 NaN3 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 9.3X10(5) daltons, composed of identical subunits of 7X10(4) 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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Ishihama A,Ikeuchi T,Matsumoto A,Yamamoto S

doi

10.1093/oxfordjournals.jbchem.a131160

keywords:

subject

Has Abstract

pub_date

1976-05-01 00:00:00

pages

927-37

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

79

pub_type

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