Abstract
The purified G-proteins from bovine brain were examined for potential solubility in the absence of detergent. The isolated α(o) and α(i) subunits migrated through sucrose with rates consistent with the existence of monomeric species either in the presence or the absence of cholate. The βγ subunits or holo-G-proteins aggregated extensively if cholate was absent. Al3+, Mg2+, and F- prevented the aggregation of α(o) and α(i) caused by the addition of βγ and could also prevent the aggregation of α(s) when G(s) was examined at higher temperature. The association of subunits with phospholipid vesicles was examined. Whereas βγ associated totally with phospholipid vesicles, purified α(o) showed little interaction. α(o) did bind to vesicles containing βγ (βγ vesicles) in a saturable fashion that indicated a stoichiometric association between the subunits. Treatment with guanosine 5'-(3-O-thio)triphosphate could partially dissociate α(o) that was bound to βγ vesicles. These data suggest that βγ may be an anchor for association of α subunits with membranes and that regulation by these proteins may not be limited to the plasma membrane. This possibility and its implications are discussed. The reversible association of α(o) to βγ vesicles may provide a very sensitive system for the study of the interactions between these subunits.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 631-637 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 261 |
| Issue number | 2 |
| State | Published - 1986 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
The purified α subunits of G(o) and G(i) from bovine brain require βγ for association with phospholipid vesicles. / Sternweis, P. C.
In: Journal of Biological Chemistry, Vol. 261, No. 2, 1986, p. 631-637.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The purified α subunits of G(o) and G(i) from bovine brain require βγ for association with phospholipid vesicles
AU - Sternweis, P. C.
PY - 1986
Y1 - 1986
N2 - The purified G-proteins from bovine brain were examined for potential solubility in the absence of detergent. The isolated α(o) and α(i) subunits migrated through sucrose with rates consistent with the existence of monomeric species either in the presence or the absence of cholate. The βγ subunits or holo-G-proteins aggregated extensively if cholate was absent. Al3+, Mg2+, and F- prevented the aggregation of α(o) and α(i) caused by the addition of βγ and could also prevent the aggregation of α(s) when G(s) was examined at higher temperature. The association of subunits with phospholipid vesicles was examined. Whereas βγ associated totally with phospholipid vesicles, purified α(o) showed little interaction. α(o) did bind to vesicles containing βγ (βγ vesicles) in a saturable fashion that indicated a stoichiometric association between the subunits. Treatment with guanosine 5'-(3-O-thio)triphosphate could partially dissociate α(o) that was bound to βγ vesicles. These data suggest that βγ may be an anchor for association of α subunits with membranes and that regulation by these proteins may not be limited to the plasma membrane. This possibility and its implications are discussed. The reversible association of α(o) to βγ vesicles may provide a very sensitive system for the study of the interactions between these subunits.
AB - The purified G-proteins from bovine brain were examined for potential solubility in the absence of detergent. The isolated α(o) and α(i) subunits migrated through sucrose with rates consistent with the existence of monomeric species either in the presence or the absence of cholate. The βγ subunits or holo-G-proteins aggregated extensively if cholate was absent. Al3+, Mg2+, and F- prevented the aggregation of α(o) and α(i) caused by the addition of βγ and could also prevent the aggregation of α(s) when G(s) was examined at higher temperature. The association of subunits with phospholipid vesicles was examined. Whereas βγ associated totally with phospholipid vesicles, purified α(o) showed little interaction. α(o) did bind to vesicles containing βγ (βγ vesicles) in a saturable fashion that indicated a stoichiometric association between the subunits. Treatment with guanosine 5'-(3-O-thio)triphosphate could partially dissociate α(o) that was bound to βγ vesicles. These data suggest that βγ may be an anchor for association of α subunits with membranes and that regulation by these proteins may not be limited to the plasma membrane. This possibility and its implications are discussed. The reversible association of α(o) to βγ vesicles may provide a very sensitive system for the study of the interactions between these subunits.
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UR - http://www.scopus.com/inward/citedby.url?scp=0022608859&partnerID=8YFLogxK
M3 - Article
C2 - 3079758
AN - SCOPUS:0022608859
VL - 261
SP - 631
EP - 637
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 2
ER -