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(Received for publication, April 16, 1997, and in revised form, August 4, 1997)
From the ADP-ribosylation factors (ARFs) are highly
conserved ~20-kDa guanine nucleotide-binding proteins that enhance
the ADP-ribosyltransferase activity of cholera toxin and are believed
to participate in vesicular transport in both exocytic and endocytic
pathways. Several ARF-like proteins (ARLs) have been cloned from
Drosophila, rat, and human; however, the biological
functions of ARLs are unknown. We have identified a yeast gene
(ARL1) encoding a protein that is structurally related
(>60% identical) to human, rat, and Drosophila ARL1.
Biochemical analyses of purified recombinant yeast ARL1 (yARL1) protein
revealed properties similar to those ARF and ARL1 proteins, including
the ability to bind and hydrolyze GTP. Like other ARLs, recombinant yARL1 protein did not stimulate cholera toxin-catalyzed
auto-ADP-ribosylation. yARL1 was not recognized by antibodies against
mammalian ARLs or yeast ARFs. Anti-yARL1 antibodies did not cross-react
with yeast ARFs, but did react with human ARLs. On subcellular
fractionation, yARL1, similar to yARF1, was localized to the soluble
fraction. The amino terminus of yARL1, like that of ARF, was
myristoylated. Unlike Drosophila Arl1, yeast
ARL1 was not essential for cell viability. Like rat ARL1,
yARL1 might be associated in part with the Golgi complex. However,
yARL1 was not required for endoplasmic reticulum-to-Golgi protein
transport, and it may offer an opportunity to define an ARL function in
another kind of vesicular trafficking, such as the regulated secretory
pathway.
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30998-31005
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Characterization of an ADP-ribosylation Factor-like 1 Protein in
Saccharomyces cerevisiae
,
,
,
,
,
,
Institute of Molecular Medicine, School of
Medicine, National Taiwan University, Taipei, Taiwan, Republic of China
and the ¶ Pulmonary-Critical Care Medicine Branch, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892-1434
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