TY - JOUR
T1 - Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain
AU - Sternweis, P. C.
AU - Robishaw, J. D.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1984
Y1 - 1984
N2 - Membranes from bovine brain bind relatively large quantities of guanosine 5'-(3-O-thio)triphosphate (GTPγS) with high affinity. The two proteins responsible for most of this activity were purified; they account for 1.5% of the membrane protein. The two proteins contain α subunits of either 39,000 and 41,000 Da, β subunits of 36,000 or 35,000 Da, and a potential γ subunit (11,000 Da). These structures are the same as a family of proteins that includes transducin and the regulatory proteins, G(S) and G(I), of adenylate cyclase. The 41,000- and 39,000-Da polypeptides can be ADP-ribosylated with islet-activating protein from Bordetella pertussis, bind guanine nucleotides specifically, and migrate through polyacrylamide gels with rates similar to the α subunits of G(I) and transducin, respectively. The 36,000- and 35,000-Da polypeptides are similar to the β subunits of G(I) and G(S). The γ subunit is found whenever β subunits are present. The 41,000- and 39,000-Da polypeptides (with β and γ) are designated, respectively, G(I) and G(O) from brain. The α subunit of G(O) was isolated without the use of ligands known to dissociate other G proteins. G(O)α binds GTPγS reversible in the absence of Mg2+ and is relatively stable in cholate. This isolated α subunit should be of great utility in elucidating the mechanism of action of this family of GTP-binding proteins.
AB - Membranes from bovine brain bind relatively large quantities of guanosine 5'-(3-O-thio)triphosphate (GTPγS) with high affinity. The two proteins responsible for most of this activity were purified; they account for 1.5% of the membrane protein. The two proteins contain α subunits of either 39,000 and 41,000 Da, β subunits of 36,000 or 35,000 Da, and a potential γ subunit (11,000 Da). These structures are the same as a family of proteins that includes transducin and the regulatory proteins, G(S) and G(I), of adenylate cyclase. The 41,000- and 39,000-Da polypeptides can be ADP-ribosylated with islet-activating protein from Bordetella pertussis, bind guanine nucleotides specifically, and migrate through polyacrylamide gels with rates similar to the α subunits of G(I) and transducin, respectively. The 36,000- and 35,000-Da polypeptides are similar to the β subunits of G(I) and G(S). The γ subunit is found whenever β subunits are present. The 41,000- and 39,000-Da polypeptides (with β and γ) are designated, respectively, G(I) and G(O) from brain. The α subunit of G(O) was isolated without the use of ligands known to dissociate other G proteins. G(O)α binds GTPγS reversible in the absence of Mg2+ and is relatively stable in cholate. This isolated α subunit should be of great utility in elucidating the mechanism of action of this family of GTP-binding proteins.
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M3 - Article
C2 - 6438083
AN - SCOPUS:0021748090
SN - 0021-9258
VL - 259
SP - 13806
EP - 13813
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 22
ER -