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(Received for publication, April 16, 1996, and in revised form, May 28, 1996)
From the The native V1 complex of the tobacco
hornworm vacuolar type ATPase (V-ATPase) was purified from cytosolic
extracts of molting larval midgut. It consisted of the established
V-ATPase subunits A, B, and E along with the 14-kDa subunit F and the
novel 13-kDa subunit G. The final amount of purified V1
complex made up an unexpectedly high 2% of the total cytosolic
protein, with a yield of ~0.4 mg/g of tissue. An equally high amount
of cytosolic V1 complex was obtained from starving
intermolt larvae. By contrast, the cytosolic V1 pool was
reduced drastically in feeding intermolt larvae or in larvae that had
been refed after starvation. The activity of the membrane-bound
V-ATPase holoenzyme was inversely related to the size of the cytosolic
V1 pool, suggesting that the insect plasma membrane
V-ATPase is regulated by reversible disassembly of the V1
complex as a function of the feeding condition of the larvae. Like
F1-ATPases, the purified V1 complex exhibited
Ca2+-dependent ATPase activity and, in the
presence of 25% methanol, exhibited
Mg2+-dependent ATPase activity. Therefore, we
designate the native V1 complex, V1-ATPase.
Both enzyme activities were completely inhibited by micromolar
N-ethylmaleimide. In contrast to the
Ca2+-dependent V1-ATPase activity,
the Mg2+/methanol-dependent
V1-ATPase activity did not decrease with the incubation
time and thus was not inhibited by ADP. Methanol appears to induce a
conformational change of the V1 complex, leading to
enzymatic properties of the V1-ATPase that are similar to
those of the membrane-bound V-ATPase holoenzyme. This is the first time
that a native and enzymatically active V1 complex has been
purified from the cytosol.
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20908-20913
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
Zoologisches Institut der Universität
München, Luisenstrasse 14, D-80333 München, Germany and
the § Department of Biology, Temple University,
Philadelphia, Pennsylvania 19122
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