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An Arabidopsis VPS45p Homolog Implicated in Protein Transport to
the Vacuole1
Diane C. Bassham and
Natasha V. Raikhel*
Michigan State University-Department of Energy Plant Research
Laboratory, Michigan State University, East Lansing, Michigan
48824-1312
The Sec1p family of proteins is
required for vesicle-mediated protein trafficking between various
organelles of the endomembrane system. This family includes Vps45p,
which is required for transport to the vacuole in yeast
(Saccharomyces cerevisiae). We have isolated a cDNA
encoding a VPS45 homolog from Arabidopsis
thaliana (AtVPS45). The cDNA is able to
complement both the temperature-sensitive growth defect and the
vacuolar-targeting defect of a yeast vps45 mutant,
indicating that the two proteins are functionally related. AtVPS45p is
a peripheral membrane protein that associates with microsomal
membranes. Sucrose-density gradient fractionation demonstrated that
AtVPS45p co-fractionates with AtELP, a potential vacuolar protein
sorting receptor, implying that they may reside on the same membrane
populations. These results indicate that AtVPS45p is likely to function
in the transport of proteins to the vacuole in plants.
1
This research was supported by grants from the
National Science Foundation (no. MCB-9507030) and the U.S. Department
of Energy (no. DE-FG02-91ER-20021) to N.V.R.
*
Corresponding author; e-mail nraikhel{at}pilot.msu.edu; fax
1-517-353-9168.
Plant Physiol. (1998) 117: 407-415
Copyright Clearance Center: 0032-0889/98/117/0407/09
© 1998 American Society of Plant Physiologists
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