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J Biol Chem, Vol. 274, Issue 25, 17417-17423, June 18, 1999
From the Pulmonary-Critical Care Medicine Branch, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892
A brefeldin A (BFA)-inhibited guanine
nucleotide-exchange protein (GEP) for ADP-ribosylation factors (ARF)
was purified earlier from bovine brain cytosol. Cloning and expression
of the cDNA confirmed that the recombinant protein (p200) is a
BFA-sensitive ARF GEP. p200 contains a domain that is 50% identical in
amino acid sequence to a region in yeast Sec7, termed the Sec7 domain. Sec7 domains have been identified also in other proteins with ARF GEP
activity, some of which are not inhibited by BFA. To identify structural elements that influence GEP activity and its BFA
sensitivity, several truncated mutants of p200 were made. Deletion of
sequence C-terminal to the Sec7 domain did not affect GEP activity. A
protein lacking 594 amino acids at the N terminus, as well as sequence following the Sec7 domain, also had high activity. The mutant lacking
630 N-terminal amino acids was, however, only 1% as active, as was the
Sec7 domain itself (mutant lacking 697 N-terminal residues). It appears
that the Sec7 domain of p200 contains the catalytic site but additional
sequence (perhaps especially that between positions 595 and 630)
modifies activity dramatically. Myristoylated recombinant ARFs were
better than non-myristoylated as substrates; ARFs 1 and 3 were better
than ARF5, and no activity was detected with ARF6. Physical interaction
of the Sec7 domain with an ARF1 mutant was demonstrated, but it was
much weaker than that of the cytohesin-1 Sec7 domain with the same ARF
protein. Effects of BFA on p200 and all mutants with high activity were
similar with ~50% inhibition at 
50 µM. The
inactive BFA analogue B36 did not inhibit the Sec7 domain or p200.
Thus, the Sec7 domain of p200, like that of Sec7 itself (Sata, M.,
Donaldson, J. G., Moss, J., and Vaughan, M. (1998) Proc.
Natl. Acad. Sci. U. S. A. 95, 4204-4208), plays a role in BFA
inhibition as well as in GEP activity, although the latter is markedly
modified by other structural elements.
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