The GTPase superfamily: a conserved switch for diverse cell functions

HR Bourne, DA Sanders, F McCormick - Nature, 1990 - nature.com
HR Bourne, DA Sanders, F McCormick
Nature, 1990nature.com
Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate.
Each of these many GTPases acts as a molecular switch whose'on'and'off states are
triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad
versions of the switch—in bacteria, yeast, flies and vertebrates—suggest that all derive from
a single primordial protein, repeatedly modified in the course of evolution to perform a
dazzling variety of functions.
Abstract
Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch—in bacteria, yeast, flies and vertebrates—suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions.
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