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J Biol Chem, Vol. 274, Issue 34, 24054-24058, August 20, 1999

Tubulin Folding Cofactors as GTPase-activating Proteins
GTP HYDROLYSIS AND THE ASSEMBLY OF THE /-TUBULIN HETERODIMER

From the Department of Biochemistry, New York University Medical Center, New York, New York 10016

In vivo, many proteins must interact with molecular chaperones to attain their native conformation. In the case of tubulin, newly synthesized - and -subunits are partially folded by cytosolic chaperonin, a double-toroidal ATPase with homologs in all kingdoms of life and in most cellular compartments. - and -tubulin folding intermediates are then brought together by tubulin-specific chaperone proteins (named cofactors A-E) in a cofactor-containing supercomplex with GTPase activity. Here we show that tubulin subunit exchange can only occur by passage through this supercomplex, thus defining it as a dimer-making machine. We also show that hydrolysis of GTP by -tubulin in the supercomplex acts as a switch for the release of native tubulin heterodimer. In this folding reaction and in the related reaction of tubulin-folding cofactors with native tubulin, the cofactors behave as GTPase-activating proteins, stimulating the GTP-binding protein -tubulin to hydrolyze its GTP.

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