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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 Mannoproteins, which are one type of
the components of the Saccharomyces cerevisiae cell wall,
can be divided into three groups: sodium dodecyl sulfate
(SDS)-extractable, reducing-reagent-extractable, and
glucanase-extractable mannoproteins (5, 12, 23).
Glucanase-extractable mannoproteins are covalently bound to
GPI-associated proteins have several common structural characteristics:
a signal sequence for secretion in the N terminus and a GPI signal for
attachment to GPI in the C terminus. The GPI signal itself has three
domains: the region containing the GPI attachment site (the Nucleotide sequences.
The Saccharomyces Genome
Database was used as a source of nucleotide and amino acid sequences of
all the ORFs examined, except for YBR078W. Our sequence analysis of
YBR078W identified an insertion of C at nucleotide position 1610, resulting in reduction of the ORF size from 468 to 429 amino acids. The
C-terminal amino acid sequence used for YBR078W is shown in Table
1.
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
ABSTRACT
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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.
INTRODUCTION
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
-1,6-glucan of the cell wall, which forms a large complex with
-1,3-glucan and chitin (9, 10, 11, 13, 17, 19, 20). Many
genes encoding glucanase-extractable cell wall mannoproteins have been
isolated from Saccharomyces cerevisiae, and so far most of
them have been identified as glycosylphosphatidylinositol
(GPI)-dependent cell wall proteins (15, 16, 18, 21, 24, 26, 28,
31, 32).
site)
plus the first and second amino acids downstream of the site, a
spacer of 5 to 10 amino acids, and a hydrophobic stretch of 10 to 15 amino acids (22, 29). A protein containing the GPI signal is
cleaved at the site, and the resulting carboxy terminus of the
protein is covalently bound to a GPI moiety (23, 30). This
reaction occurs in the endoplasmic reticulum. Being associated with
membranes by means of the GPI moiety, GPI-attached proteins are then
transported to the cell surface and remain on the plasma membrane as
GPI-anchored proteins; however, some of them are further processed.
They are incorporated into the cell wall by detaching themselves from
the GPI moiety and then by linking themselves to -1,6-glucan of the cell wall (6, 30). These different processes suggest that each GPI-attached protein has a signal for selecting either to be
incorporated into the cell wall or to remain on the plasma membrane.
Two kinds of amino acid sequences in the region upstream of the site (the -minus region) have been proposed as being responsible for
the selection: dibasic residues for remaining on the plasma membrane
(3, 33) and specific amino acid residues at sites 4 or 5 and
2 amino acids upstream of the site (-4/5 and -2 sites,
respectively) for incorporation into the cell wall (7). The
former residues were determined by sequence analysis, and the latter
residues were determined by mutational analysis mainly by using
synthetic model sequences. We now need to evaluate these proposals with
more authentic sequences of GPI-attached proteins. A number of open
reading frames (ORFs) encoding putative GPI-attached proteins have been
selected from previous studies (3, 8). In this study, we
quantitatively measured the cell wall incorporation of fusion reporter
proteins that were constructed from these ORFs and examined the
relationship between efficiencies of cell wall incorporation and amino
acid residues in their -minus regions.
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
TABLE 1.
Efficiencies of incorporation of the fusion reporter
proteins into cell walls
Expression of a fusion reporter protein.
A DNA fragment
covering the most C-terminal 40 amino acids of a GPI-attached protein
and about 200 bp of its 3' noncoding region was amplified by PCR with
primers containing a SalI or BamHI restriction
site. The resulting fragment was inserted into the SalI and
BamHI sites of a multicopy plasmid, pE
GALHA
(8). pEGALHA contains a reporter gene comprising the
signal sequence of yeast invertase, the -galactosidase from
Cyamopsis tetragonoloba, and a hemagglutinin (HA) epitope.
The plasmid containing the fusion reporter gene was used to transform
the yeast strain YPH499 (27).
Construction of genes encoding GPI proteins tagged with HA. A fragment containing the 400 bp of the 5' noncoding region and the N-terminal 25 amino acids of Yer150w was amplified by PCR and inserted into the SacI and BamHI sites of a plasmid, pEHA. pEHA contains the triple-HA epitope sequence between the BamHI and SalI sites of the multicloning site of a multicopy plasmid, YEplac195 (7). Another fragment containing the C-terminal 122 amino acids of Yer150w and the 300 bp of its 3' noncoding region was amplified by PCR and inserted into the SalI and HindIII sites, generating pEHAYer150w. Similarly, the triple-HA epitope sequence was inserted in frame into the 25th amino acid position of the Yor382w sequence on pEHAYor382w.
Analysis of cell wall-associated proteins. Cell walls were isolated from yeast transformant cells grown in a selection medium. The yeast cells were broken with glass beads in LY buffer (50 mM Tris-HCl [pH 7.4], 150 mM NaCl, 5 mM EDTA, 1 mM phenylmethylsulfonyl fluoride) containing 2% SDS. The pellet generated by centrifugation was twice treated with hot 2% SDS in LY buffer by heating it for 10 min at 95°C each time, followed by washing it five times with LM buffer (100 mM sodium acetate [pH 5.5], 1 mM EDTA, 1 mM phenylmethylsulfonyl fluoride). The washed cell walls were incubated with laminarinase (product no. L5144; Sigma) at a concentration of 0.25 U/ml twice for 1 h each time at 37°C. The treated sample was centrifuged in a microcentrifuge at 10,000 rpm for 2 min at 4°C, and the resulting supernatant was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting. Protein bands on the blots were detected with the anti-HA monoclonal antibody 12CA5 (Boehringer Mannheim). The band intensities were measured with an Image Master ID (Pharmacia Biotech) and were represented as mean values with standard deviations from measurements of four different transformants.
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RESULTS |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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The most C-terminal 40 amino acid sequence of each ORF was fused
to a reporter protein comprising the invertase signal sequence, an
-galactosidase from guar, and an HA epitope. The fusion reporter gene is transcribed by the PGK1 promoter (8). A
plasmid containing the fusion reporter gene was introduced into the
yeast strain YPH499. Cell wall fractions were isolated from each
transformant, digested with glucanase, and analyzed on Western blots.
The amounts of glucanase-extracted fusion reporter proteins were
measured, and the ratios of their amounts to the total amounts of
fusion reporter proteins in cells were calculated (Table 1). Table 1 also shows the amino acid sequences of ORFs used to construct the
fusion reporter genes. Among the 34 fusion reporter proteins examined,
15 have amino acid residues of I, V, or L at the -4/5 site and Y or
N at the -2 site, 11 have the basic amino acid residues K and R or K
alone in the short -minus region, and the remaining 8 have none of
these distinguishing residues. These fusion reporter proteins were
incorporated into the cell wall in various ratios from 0.421 for the
fusion reporter protein of Ydr534c (FP-Ydr534c) to 0.042 for
FP-Yol132w. Fusion reporter proteins constructed from two
well-characterized GPI-dependent cell wall proteins, Sed1p (also called
Ydr077w) (25, 32) and Ag1p/Yjr004c (19, 34),
showed ratios of 0.297 and 0.265, respectively, while that of a
well-characterized GPI-dependent plasma membrane protein, Yap3p/Ylr120c
(1, 4, 14), showed a ratio of 0.051. A histogram based on
the results in Table 1 clearly indicates the correlation between
efficiencies of cell wall incorporation and sequences in the -minus
region (Fig. 1): cell wall incorporation
was higher in the fusion reporter proteins containing the specific
amino acid residues I, V, or L at the -4/5 site and Y or N at the
-2 site than in those containing no such specific amino acid
residues.
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4/5 and 2); sequences with
two basic amino acid residues R and/or K in the Two proteins, Yer150w, which has V at the -5 site and N at the -2
site, and Yor382w, which has a stretch of serine residues in the
-minus region, were examined for their cell wall incorporation. An
HA epitope was inserted at the 25th amino acid position from the first
methionine of each protein, generating the HA-tagged proteins
Yer150w-HA and Yor382w-HA, and their cellular localization was
examined. Of the total amount of Yer150w-HA protein, 12.7% was
detected as glucanase-extractable cell wall protein (Fig. 2A). This level was much higher than that
of Yor382w-HA. The amount of Yor382w-HA released from the cell wall by
glucanase was only 2.9% of the total amount of Yor382-HA protein in
the cells (Fig. 2B). Yer150w-HA has three potential N-glycosylation
sites, while Yor382w-HA has not. Consistent with these characteristics,
the Yer150w-HA bands appeared differently on Western blots before and
after endoglycosidase H treatment (Fig. 2A, lanes 3 and 4), while the
Yor382w-HA bands appeared to be unchanged before and after the
treatment (data not shown). These results suggested that N
glycosylation occurs at least at one of the three potential sites in
Yer150w-HA.
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DISCUSSION |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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We demonstrated in a previous study that the amino acid sequences
at the -minus region are important for the determination of the
final cellular localization of GPI-attached proteins and that the amino
acid residues V or I at the -4/5 site and V, I, N, or Y at the -2
site are required for the efficient incorporation of GPI-attached
proteins into the cell wall (7). This requirement, called
the -4/5 and -2 rule, was identified through a mutational analysis of synthetic -minus regions. In this study, this rule was
verified, as shown in the histogram of Fig. 1. Fusion reporter proteins
which have the specific amino acid residues of I, V, or L at the -5
site and Y or N at the -2 site were incorporated into the cell wall
with greater efficiency than those which have no specific amino acid
residues in the short -minus region. A similar correlation was also
observed for intact proteins tagged with HA. The level of cell wall
incorporation of Yer150w-HA was much higher than that of Yor382w-HA.
Yer150w meets the rule, while Yor382 does not. Our results clearly
indicate that these specific residues function as a signal that
enhances the incorporation efficiency of GPI-attached proteins into the
cell wall. Furthermore, in keeping with the previous findings that
replacement of S with Y in a synthetic sequence comprising a serine
stretch partially enhances cell wall incorporation (7),
efficiencies of the cell wall incorporation of FP-Yir019c and
FP-Ypl130w, both of which have only Y at the -2 site, were
comparable to those of fusion reporter proteins containing the specific
amino acid residues in both of the -4/5 and -2 sites. This
suggests that specific amino acid residues only at the -2 site in
some sequences may be enough for efficient incorporation of GPI
proteins into the cell wall. To reach a conclusion, however, further
examination will be required.
Levels of glucanase-extractable cell wall proteins varied among the
fusion reporter proteins with the specific amino acid residues,
suggesting that some factors other than those of the -4/5 and -2
rule may modify the efficiency of cell wall incorporation. These
factors are probably governed by the amino acid sequences themselves,
and it is possible that glycosylation of proteins may be one of these
factors. However, N glycosylation would be excluded from the
possibility. Among the 15 ORFs, YOR214C, YPL130W, YLR110C, and
YNL300W have potential N-glycosylation sites within the sequences used
for the construction of the fusion reporter proteins (Table 1). In
fact, their fusion reporter proteins were detected as broad and smeared
bands at considerably higher molecular-mass positions on Western blots
(data not shown). Ratios of cell wall incorporation were 0.338, 0.315, 0.220, and 0.214 for FP-Yor214c, FP-Ypl130w, FP-Ylr110c, and
FP-Ynl300w, respectively, indicating that there is no correlation
between N glycosylation and levels of cell wall incorporation. In our
previous study, Ypl130w was not classified as a putative GPI-dependent
cell wall protein, because the fusion protein was not detected in the
cell wall fraction treated with glucanase (8). In this
study, it was clearly detected. This difference in detection may be due
to difficulties in detecting N-glycosylated proteins on Western blots.
On the other hand, it is possible that O glycosylation of proteins may
partly explain the diversity of cell wall incorporation. Considering
the S/T richness of the -minus regions, it is likely that the fusion reporter proteins are O glycosylated to various extents. Deletion of
several genes required for O glycosylation has been known to affect the incorporation efficiency of GPI-attached proteins into the
cell wall (2). Further examinations are needed to reach a conclusion.
Vossen et al. have suggested from sequence analysis that a dibasic
motif in the -minus region may participate in a signal for detaining
GPI-attached proteins on the plasma membrane (33). Our
results support this proposal. As clearly shown in Fig. 1, incorporation ratios of all the fusion reporter proteins that contain
two basic amino acid residues in the -minus region into the cell
wall were quite low. These ratios were lower than those of the fusion
reporter proteins that did not have the two basic amino acid residues.
Furthermore, all of the fusion reporter proteins examined in this study
were detected in a detergent phase by phase separation with Triton
X-114, and the proteins extracted in the detergent phase were
phosphatidylinositol-phospholipase C sensitive (data not shown),
indicating GPI attachment. Therefore, it can be concluded that with
fusion reporter proteins with two basic amino acid residues in the
-minus region, nearly all the amounts of their proteins remain on
the plasma membrane in a GPI-associated form. These two basic residues
probably function as a negative factor in the process of cell wall incorporation.
Taken together, these results indicate that GPI-attached proteins have
two different signals for determining their cellular localization.
These are the amino acid residues V, I, or L at the -4/5 site and Y
or N at the -2 site and the basic residue(s) R and/or K in the short
-minus region. The former residues act as a positive factor for cell
wall incorporation, while the later residues act as a negative factor
for incorporation, such that the proteins remain on the plasma membrane
as GPI-anchored proteins.
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ACKNOWLEDGMENT |
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We thank S. Bernice Miwa for critical reading of the manuscript.
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FOOTNOTES |
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* 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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Abstract
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Materials and Methods
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Discussion
References
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Journal of Bacteriology, July 1999, p. 3886-3889, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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