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J Biol Chem, Vol. 273, Issue 5, 2553-2560, January 30, 1998
From the Pulmonary-Critical Care Medicine Branch, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892
ADP-ribosylation factors (ARFs) are ~20-kDa
guanine nucleotide-binding proteins recognized as critical components
in intracellular vesicular transport and phospholipase D activation.
Both guanine nucleotide-exchange proteins and GTPase-activating
proteins (GAPs) for ARFs have been cloned recently. A zinc finger motif
near the amino terminus of the ARF1 GAP was required for stimulation of GTP hydrolysis. ARD1 is an ARF family member that differs from other
ARFs by the presence of a 46-kDa amino-terminal extension. We had
reported that the ARF domain of ARD1 binds specifically GDP and GTP and
that the amino-terminal extension acts as a GAP for the ARF domain of
ARD1 but not for ARF proteins. The GAP domain of ARD1, synthesized in
Escherichia coli, stimulated hydrolysis of GTP bound to the
ARF domain of ARD1. Using ARD1 truncations, it appears that amino acids
101-190 are critical for GAP activity, whereas residues 190-333 are
involved in physical interaction between the two domains of ARD1 and
are required for GTP hydrolysis. The GAP function of the amino-terminal
extension of ARD1 required two arginines, an intact zinc finger motif,
and a group of residues which resembles a sequence present in
Rho/Rac GAPs. Interaction between the two domains of ARD1
required two negatively charged residues (Asp427 and
Glu428) located in the effector region of the ARF domain
and two basic amino acids (Arg249 and Lys250)
found in the amino-terminal extension. The GAP domain of ARD1 thus
is similar to ARF GAPs but differs from other GAPs in its covalent association with the GTP-binding domain.
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