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J. Biol. Chem., Vol. 265, Issue 4, 2383-2390, 02, 1990
PJ Casey, HK Fong, MI Simon and AG Gilman
Cloning of a complementary DNA (cDNA) for Gz alpha, a newly appreciated
member of the family of guanine nucleotide-binding regulatory proteins (G
proteins), has allowed preparation of specific antisera to identify the
protein in tissues and to assay it during purification from bovine brain.
Additionally, expression of the cDNA in Escherichia coli has resulted in
the production and purification of the recombinant protein. Purification of
Gz from bovine brain is tedious, and only small quantities of protein have
been obtained. The protein copurifies with the beta gamma subunit complex
common to other G proteins; another 26- kDa GTP-binding protein is also
present in these preparations. The purified protein could not serve as a
substrate for NAD-dependent ADP- ribosylation catalyzed by either pertussis
toxin or cholera toxin. Purification of recombinant Gz alpha (rGz alpha)
from E. coli is simple, and quantities of homogeneous protein sufficient
for biochemical analysis are obtained. Purified rGz alpha has several
properties that distinguish it from other G protein alpha subunit
polypeptides. These include a very slow rate of guanine nucleotide exchange
(k = 0.02 min-1), which is reduced greater than 20-fold in the presence of
mM concentrations of Mg2+. In addition, the rate of the intrinsic GTPase
activity of Gz alpha is extremely slow. The hydrolysis rate (kcat) for rGz
alpha at 30 degrees C is 0.05 min-1, or 200-fold slower than that
determined for other G protein alpha subunits. rGz alpha can interact with
bovine brain beta gamma but does not serve as a substrate for
ADP-ribosylation catalyzed by either pertussis toxin or cholera toxin.
These studies suggest that Gz may play a role in signal transduction
pathways that are mechanistically distinct from those controlled by the
other members of the G protein family.
Gz, a guanine nucleotide-binding protein with unique biochemical properties
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.
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