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Journal of Bacteriology, April 1999, p. 2620-2623, Vol. 181, No. 8
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Lactate-Proton Symport of Saccharomyces
cerevisiae Is Encoded by JEN1
Margarida
Casal,1
Sandra
Paiva,1
Raquel P.
Andrade,1
Carlos
Gancedo,2 and
Cecília
Leão1,*
Centro de Ciências do Ambiente,
Departamento de Biologia, Universidade do Minho, 4719 Braga Codex,
Portugal,1 and Instituto de
Investigaciones Biomédicas Alberto Sols, CSIC-UAM, 28029 Madrid,
Spain2
Received 23 October 1998/Accepted 22 January 1999
 |
ABSTRACT |
A mutant of Saccharomyces cerevisiae deficient in the
lactate-proton symport was isolated. Transformation of the mutant with a yeast genomic library allowed the isolation of the gene
JEN1 that restored lactate transport. Disruption of
JEN1 abolished uptake of lactate. The results indicate
that, under the experimental conditions tested, no other
monocarboxylate permease is able to efficiently transport lactate in
S. cerevisiae.
| |
TEXT |
Saccharomyces cerevisiae
is able to utilize short-chain monocarboxylic acids as sole carbon and
energy sources under aerobic conditions. Transport across the plasma
membrane is the first step in the metabolism of these substrates.
Monocarboxylate proton symporters with different specificities have
been described: acetic acid or ethanol-grown cells present a permease
which is shared by acetate, propionate, and formate (5),
while cells grown with lactic acid have an additional permease which
transports lactate, pyruvate, acetate, and propionate (4,
6). The capacity to transport monocarboxylates was not present
when the cells were grown in glucose (6). In agreement with
the physiological results indicating the existence of different
monocarboxylate permeases in S. cerevisiae, four open
reading frames (ORFs) with important similarities to mammalian
monocarboxylate permeases were found in the genome of S. cerevisiae (13, 16). However, to our knowledge, no
direct evidence relating a concrete gene product with a definite monocarboxylate transport activity is available. We have obtained yeast
mutants unable to transport lactic acid and have cloned a gene that
restores this transport capacity. The results presented in this work
indicate that the product of the gene JEN1 is a permease for
lactate and suggest that, under the experimental conditions analyzed,
no other system for lactate transport was operating in S. cerevisiae.
S. cerevisiae W303-1A (MATa ade2 leu2 his3
trp1 ura3) (20) was used as starting material. Its
isogenic strain of the opposite mating type was used in crosses. Yeasts
were grown in 1% (wt/vol) yeast extract-1% (wt/vol) peptone (YP) or
in 0.7% (wt/vol) Difco yeast nitrogen base (YNB) supplemented with
adequate quantities of nutrients required for growth. Carbon sources
were 2% (wt/vol) glucose, 0.5% (vol/vol) DL-lactic acid
(pH 5.0), 0.5% (wt/vol) sodium pyruvate (pH 5.0), 0.5% (vol/vol)
acetic acid (pH 5.0), 1% (wt/vol) glycerol, and 1% (wt/vol) ethanol.
To prepare solid media, 2% (wt/vol) agar was added. Growth was at
28°C, and liquid cultures were grown with shaking. Cultures were
always harvested during the exponential phase of growth.
Escherichia coli XL-Blue and DH5
were used for plasmid
amplification and preparation (19). Uptake experiments were
carried out with yeast suspensions prepared from cells growing
exponentially in YP-lactate washed twice with chilled water and
resuspended in water. Conical centrifuge tubes containing 30 µl of
0.1 M KH2PO4 buffer at pH 5.0 and 10 µl of
the yeast suspension (25 to 45 mg [dry weight]/ml) were incubated for
4 min at 25°C. Next, the reaction was started by the addition of 10 µl of an aqueous solution of labelled
DL-[1-14C]lactic acid (sodium salt; Amersham)
(3,000 dpm/nmol) at pH 5.0. The reaction was stopped by dilution with 5 ml of ice-cold water. Sampling times were 0, 5, 10, and 20 s, so
that uptake rates remained linear. The reaction mixtures were filtered
immediately through GF/C membranes (Whatman, Inc., Clifton, N.J.), and
the filters were washed with 10 ml of ice-cold water and transferred to
scintillation fluid (Opti-Phase HiSafe II; LKB FSA Laboratory Supplies,
Loughborough, United Kingdom). Radioactivity was measured in a Packard
Tri-Carb 2200 CA liquid scintillation spectrophotometer, with
disintegrations per minute correction. For nonspecific 14C
adsorption, labelled lactate was added at zero time after the cold
water. To determine the transport kinetics best fitting the experimental initial uptake rates and to estimate the kinetic parameters, a computer-assisted nonlinear regression analysis (GraphPAD
Software, San Diego, Calif.) was used. All the experiments were
repeated at least three times. Proton uptake was measured in a
thermostated chamber at 25°C with a standard pH meter connected to a
recorder. To the chamber, 4.5 ml of 10 mM
KH2PO4 and 0.5 ml of cell suspension were
added, and the pH was adjusted to the desired value to obtain a
baseline. The lactate solution, adjusted to the same pH value, was
added and the subsequent alkalization was monitored. Rates of proton
uptake were calculated from the slope of the initial part of the pH
trace. Calibration was performed with HCl.
A commercial S. cerevisiae genomic library in YEp13 (ATCC
37323) was used. Transformation of yeast cells and molecular biology operations were performed according to the methods of Ausubel et al.
(1). Disruption of the cloned gene was done by replacing the
1,758-bp HpaI-Eco47III sequence by a 1,472-bp
PvuII-PvuII fragment from vector YDpH
(2) carrying the HIS3 gene. A 2.7-kb XbaI-ScaI fragment was used to replace the
genomic copy of the gene by the one-step disruption method
(18) (Fig. 1). Northern blot
analysis of JEN1 expression was performed according to
standard procedures (19).
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FIG. 1.
Scheme of the yeast genomic DNA region containing
JEN1 and Southern blot analysis of its disruption. (a)
Schematic restriction map of the yeast genomic DNA fragment contained
in the plasmid pT12. This plasmid, which contains the complete sequence
of JEN1 (YKL 217w), was isolated from the original YEp13
genomic library. (b) Disruption of JEN1 was carried out as
described in the text. The 2.7-kb SacI-XbaI
fragment was used to replace the genomic wild-type copy. (c) Southern
blot analysis of the JEN1 disruption. Genomic DNA was
digested with HindIII, subjected to electrophoresis in a
0.8% agarose gel, transferred to Hybond-N membrane, and hybridized
with the 855-bp probe indicated in panels a and b. Lanes: 1, DNA from
wild type; 2, DNA from BLC 203 strain carrying the
jen1::HIS3 disruption. Sizes of the fragments are
indicated at left.
|
|
Isolation and characterization of a mutant unable to grow on
DL-lactate.
A suspension of about 107
yeast cells/ml was irradiated with a UV germicidal lamp, plated on
YP-glycerol, and replica plated onto YNB-lactate. Four colonies unable
to grow in this medium were found, but only one appeared affected in
its capacity to transport lactate. A diploid isolated from a cross of
this mutant with a wild-type strain grew on lactate, indicating that
the mutation was recessive. The segregation of the negative growth on
lactate was 2+:2
in 10 complete tetrads analyzed, indicating that the phenotype was caused by a nuclear, monogenic mutation. The original mutant was named BLC 55, and a spore from a cross presenting the lactate-negative phenotype was termed BLC 142. In both cases, faint,
residual growth on lactate was always observed. A strain mutated in the
PCK1 gene, encoding phosphoenolpyruvate carboxykinase, or a
double mutant with alterations in the CYB2 and
DLD genes (12), encoding the D- and
L-lactate ferricytochrome c oxidoreductases, respectively, gave a complete absence of growth in the same medium. Strains BLC 55 and BLC 142 grew in glycerol, ethanol, or acetate as did
the wild type, but they did not grow in pyruvate.
Cells from the BLC 142 mutant grown in glucose and incubated in
YP-lactate for 4 h showed at 2.0 mM lactate a transport activity that was only one-fifth that of the wild type. Moreover, the transient extracellular alkalization indicative of proton uptake was absent after
addition of DL-lactate or pyruvate (not shown). The
observed lactate uptake could be due to diffusion of the undissociated acid. This behavior was similar to that found in glucose-repressed cells of the wild type, where no measurable activity of the lactate permease is found (6).
Isolation of the gene responsible for the lactate-negative
phenotype.
The gene whose mutation caused inability to grow in
lactate was isolated by functional complementation of strain BLC 142. The yeast was transformed to leucine prototrophy, and transformants were screened for growth on lactate. Among 20,000 transformants, 20 were able to grow efficiently on DL-lactate. When these
clones were grown under nonselective conditions, the ability to grow in
lactate and the Leu+ phenotypes were lost together in one
clone. Plasmid DNA was prepared from this transformant and used to
transform again the original BLC 142 strain. The plasmid (pT12)
restored the ability to grow in lactate, the permease activity, and the
capacity to alkalinize the medium after addition of the acid (not
shown). By restriction analysis, a yeast genomic DNA insert of 4.4 kb
was identified in pT12 (Fig. 1a). It seems, therefore, that the DNA on
the plasmid carries the gene encoding the lactate permease. A 0.9-kb
EcoRI-BamHI yeast genomic DNA fragment contained
in the pT12 plasmid was sequenced. It was found to have a sequence of
nucleotides in the vicinity of ORF YKL217w (21). This ORF
corresponds to a gene termed JEN1 that in the YPD database
is said to be implicated in the transport of lactate. The restriction
analysis of pT12 indicated that it contained JEN1. This gene
has been described as a protein member of the major facilitator
superfamily belonging to the sialate:H+ family (13,
15). It is also apparently similar to the E. coli
genes encoding the osmoregulatory proline-betaine transporter proP and
the -ketoglutarate transporter (10). It is likely that
different search algorithms recognize diverse features and produce
different assignments within a superfamily, in this case the major
facilitator superfamily (15).
Effects of the disruption of the JEN1 gene.
To
ascertain the physiological role of the JEN1 gene, we
disrupted it and placed the disrupted copy into the genome (Fig. 1b).
Southern blot analysis demonstrated that the integration was correct
(Fig. 1c). The disruptant, BLC 203, did not grow on lactate and did not
show measurable permease activity (Fig.
2a). In contrast, transport of acetate
was operational in the mutant BLC 203 under all derepressed conditions
tested (data not shown), confirming previous results which indicated
that the transport system for acetate was always present in
derepression conditions but could not transport lactate.
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FIG. 2.
Eadie-Hoffstee plots of the initial uptake rates of
lactate by the wild type and a jen1::HIS3
disrupted strain. Uptake studies were done at pH 5.0 as described in
the text. (a) Cells growing exponentially in YNB-glucose were harvested
by centrifugation, washed twice with deionized water, and incubated in
YP-lactate for 4 h. (b) Cells growing exponentially in YP-lactate.
Symbols:  , wild type;  , mutant BLC 203;  , mutant BLC 203 transformed with plasmid pT12.
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|
The mutant BLC 203 transformed with plasmid pT12 was able to grow in
YP-lactate and recovered the activity of the lactate carrier (Fig. 2b).
From the data in Fig. 2b, the following kinetics parameters were
estimated: for the wild-type, strain Vmax was estimated to be 0.40 nmol s
1 mg (dry
weight)1 and Km was estimated to
be 0.69 mM; for the BLC 203 transformed strain,
Vmax was estimated to be 0.36 nmol
s1 mg (dry weight)1 and
Km was estimated to be 0.68 mM. The fact that
the transformed strain did not transport lactate faster than the
wild-type strain could be due either to a lack of appropriate
expression or to problems with insertion of the protein in the
membrane. To distinguish between these possibilities, a Northern
analysis of the expression of JEN1 was performed (Fig.
3). After induction in YP-lactate medium,
the wild-type strain exhibited a strong signal against a
JEN1 probe while no signal was detected in noninduced cells.
Also, no signal was visible with strain BLC 203, which carries an
interrupted JEN1 gene. BLC 203 cells transformed with pT12
plasmid recovered JEN1 expression. However, in these cells, the level of JEN1 mRNA after induction was of the same order
of magnitude as that found in the wild-type strain. This finding points
to the existence of some regulatory element in the promoter that is
missing in the plasmid; in fact, it has only about 500 bp in front of
the putative ATG. The results of the Northern analysis indicate
therefore that the lack of increased transport activity in the
transformants is due to an inefficient expression.
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FIG. 3.
Northern blot analysis of JEN1 transcripts
from strains differing in locus state. JEN1, wild type;
 jen1, disruptant mutant BLC 203;
jen1(pT12), BLC 203 strain transformed with pT12 plasmid.
Total cellular mRNA was prepared from cells growing exponentially in
YNB-glucose (lane 1) and subsequently incubated in YP-lactate for
4 h (lanes 2, 3, and 4) (14). Total RNA (20 µg) was
separated on 1.5% agarose morpholinepropanesulfonic acid
(MOPS)-formaldehyde gels and blotted to nylon membranes by vacuum
transference. Hybridization was carried out using the 844-bp
NcoI-PstI fragment as a probe for JEN1
(Fig. 1a), and PDA1 (22) served as internal
standard.
|
|
The transport of lactate is an important step in the metabolism of
several organisms. In mammals, it is a key step in the reutilization by
liver and kidney of lactate produced in muscle glycolysis (the Cori
cycle). A family of monocarboxylate transporters that also transport
pyruvate and other ketoacids exists with different tissue specificities
(17). In erythrocytes, three different systems with
different mechanisms appear to operate in lactate transport, although
proton symport accounts for about 90% of it (7). In
E. coli, the lct locus, involved in lactate
metabolism, encompasses three overlapping genes, one of which
(lctP) appears to encode a lactate transporter
(8). However, to our knowledge no further information on
this system is available. Among yeasts, the mechanisms of lactate
transport are different; while Candida utilis
(11), S. cerevisiae (4, 6), and
Torulaspora delbrueckii (3) transport lactate by
proton symports, Kluyveromyces marxianus does it via a
uniport (9). It will be interesting to compare the
structures of the respective proteins involved in the process.
Our initial aim was to isolate the genes encoding the H+
symport that takes up lactate in S. cerevisiae. The results
presented here clearly show that the gene JEN1 encodes a
lactate permease and that in its absence diffusion alone does not allow
efficient growth of the yeast in lactate.
| |
ACKNOWLEDGMENTS |
We acknowledge the help of Maria J. Lafuente in the DNA sequencing
and analysis and the critical reading of the manuscript by Juana M. Gancedo.
This study was supported by Portuguese grant PRAXIS/2/2.1/BIO/1068/95.
Work in the laboratory of C.G. was supported by grant PB97-1213-CO2-01
from the Spanish CICYT. M.C. had a FEBS short-term fellowship
during the early stages of this work. S.P. received a fellowship from
PRAXIS XXI-BM4229. R.P.A. received a fellowship from PRAXIS
XXI-BD15737/98.
| |
FOOTNOTES |
*
Corresponding author. Mailing address: Centro de
Ciências do Ambiente, Departamento de Biologia, Universidade do
Minho, Campus de Gualtar, 4719 Braga Codex, Portugal. Phone:
351-53-604310. Fax: 351-53-678980. E-mail:
cleao{at}bio.uminho.pt.
| |
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Journal of Bacteriology, April 1999, p. 2620-2623, Vol. 181, No. 8
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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