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Science 17 December 1993:
Vol. 262. no. 5141, pp. 1895 - 1901
DOI: 10.1126/science.8266082
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Articles
Science, Vol 262, Issue 5141, 1895-1901
Copyright © 1993 by American Association for the Advancement of Science
Separate GTP binding and GTPase activating domains of a G alpha subunit
DW Markby,
R Onrust,
and
HR Bourne
Department of Pharmcology, University of California, San Francisco 94143.
Most members of the guanosine triphosphatase (GTPase) superfamily hydrolyze guanosine triphosphate (GTP) quite slowly unless stimulated by a GTPase activating protein or GAP. The alpha subunits (G alpha) of the heterotrimeric G proteins hydrolyze GTP much more rapidly and contain an approximately 120-residue insert not found in other GTPases. Interactions between a G alpha insert domain and a G alpha GTP-binding core domain, both expressed as recombinant proteins, show that the insert acts biochemically as a GAP. The results suggest a general mechanism for GAP-dependent hydrolysis of GTP by other GTPases.
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