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Journal of Bacteriology, July 1999, p. 3886-3889, Vol. 181, No. 13
Department of Mycology, Nippon Roche Research
Center, Kamakura, Kanagawa 247-8530, Japan
Received 10 March 1999/Accepted 29 April 1999
The final destination of glycosylphosphatidylinositol
(GPI)-attached proteins in Saccharomyces cerevisiae is the
plasma membrane or the cell wall. Two kinds of signals have been
proposed for their cellular localization: (i) the specific amino acid
residues V, I, or L at the site 4 or 5 amino acids upstream of the GPI attachment site (the
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Amino Acid Residues in the
-Minus Region
Participate in Cellular Localization of Yeast
Glycosylphosphatidylinositol-Attached Proteins
site) and Y or N at the site 2 amino acids upstream of the
site for cell wall localization and (ii) dibasic residues in the region upstream of the
site (the
-minus region) for plasma membrane localization. The relationships between these amino
acid residues and efficiencies of cell wall incorporation were examined
by constructing fusion reporter proteins from open reading frames
encoding putative GPI-attached proteins. The levels of incorporation
were high in the constructs containing the specific amino acid residues
and quite low in those containing two basic amino acid residues in the
-minus region. With constructs that contained neither specific
residues nor two basic residues, levels of incorporation were moderate.
These correlations clearly suggest that GPI-attached proteins have two
different signals which act positively or negatively in cell wall
incorporation for their cellular localization.
*
Corresponding author. Mailing address: Department of
Mycology, Nippon Roche Research Center, 200-Kajiwara, Kamakura,
Kanagawa 247-8530, Japan. Phone: 81-467-45-6752. Fax: 81-467-46-5320. E-mail: kunio.kitada{at}roche.com.
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