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J Biol Chem, Vol. 274, Issue 6, 3265-3267, February 5, 1999
From the Faculty of Pharmaceutical Sciences, Chiba University,
1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan
Properties of a membrane protein encoded by
YLL028w were examined using yeast cells transformed with
the gene. The transformed cells became resistant to polyamine toxicity,
and the resistance was overcome by bafilomycin A1, an
inhibitor of vacuolar H+-ATPase. Although spermine uptake
activity of the transformed cells was almost the same as that of wild
type cells, the uptake activity of vacuolar membrane vesicles from the
transformed cells was higher than that from wild type cells. The
transformed cells became resistant to MGBG (methylglyoxal
bis(guanylhydrazone)) and paraquat, but not Ni2+ and
Co2+, suggesting that the protein encoded by
YLL028w is a transport protein specific for polyamines.
When the YLL028w gene was disrupted by inserting the
HIS3 gene, the cells became sensitive to polyamines, and
spermine uptake activity of the vacuolar membrane vesicles decreased
significantly. The accumulated spermine in YLL028w
gene-disrupted cells decreased greatly compared with that in wild type
cells. The results indicate that a membrane protein encoded by
YLL028w (TPO1) is a polyamine transport protein
on the vacuolar membrane.
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