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PubMed2003

Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells.

Lithium is highly toxic to yeast when grown in galactose medium mainly because phosphoglucomutase, a key enzyme of galactose metabolism, is inhibited. We studied the global protein and gene expression profiles of Saccharomyces cerevisiae grown in galactose in different time intervals after addition of lithium. These results were related to physiological studies where both secreted and intracellular metabolites were determined. Microarray analysis showed that 664 open reading frames were down-regulated and 725 up-regulated in response to addition of lithium. Genes involved in transcription, translation, and nucleotide metabolism were down-regulated at the transcriptional level, whereas genes responsive to different stresses as well as genes from energy reserve metabolism and monosaccharide metabolism were up-regulated. Compared with the proteomic data, 26% of the down-regulated and 48% of the up-regulated proteins were also identified as being changed on the mRNA level. Functional clusters obtained from proteome data were coincident with transcriptional clusters. Physiological studies showed that acetate, glycerol, and glycogen accumulate in response to lithium, as reflected in expression data, whereas a change from respiro-fermentative to respiratory growth could not be predicted from the expression analyses.

Galactose↗
PubMed2006

Specific amino acids of the glycosyltransferase LpsA direct the addition of glucose or galactose to the terminal inner core heptose of Haemophilus influenzae lipopolysaccharide via alternative linkages.

Lipopolysaccharide is the major glycolipid of the cell wall of the bacterium Haemophilus influenzae, a Gram-negative commensal and pathogen of humans. Lipopolysaccharide is both a virulence determinant and a target for host immune responses. Glycosyltransferases have high donor and acceptor substrate specificities that are generally limited to catalysis of one unique glycosidic linkage. The H. influenzae glycosyltransferase LpsA is responsible for the addition of a hexose to the distal heptose of the inner core of the lipopolysaccharide molecule and belongs to the glycosyltransferase family 25. The hexose added can be either glucose or galactose and linkage to the heptose can be either beta1-2 or beta1-3. Each H. influenzae strain uniquely produces only one of the four possible combinations of linked sugar in its lipopolysaccharide. We show that, in any given strain, a specific allelic variant of LpsA directs the anomeric linkage and the added hexose, glucose, or galactose. Site-directed mutagenesis of a single key amino acid at position 151 changed the hexose added in vivo from glucose to galactose or vice versa. By constructing chimeric lpsA gene sequences, it was shown that the 3' end of the gene directs the anomeric linkage (beta1-2 or beta1-3) of the added hexose. The lpsA gene is the first known example where interstrain variation in lipopolysaccharide core structure is directed by the specific sequence of a genetic locus encoding enzymes directing one of four alternative possible sugar additions from the inner core.

Alleles↗
PubMed1986

Binding and spreading of hepatocytes on synthetic galactose culture surfaces occur as distinct and separable threshold responses.

Isolated rat hepatocytes bind to synthetic flat polyacrylamide matrices containing covalently attached galactose residues in a sugar-specific and concentration-dependent manner. Cell binding is mediated by the asialoglycoprotein receptor and occurs as a threshold response at or above a critical concentration of sugar in the matrix. Hepatocytes in the presence or absence of serum were able to spread on these synthetic galactose surfaces and were morphologically similar to cells on tissue culture plastic. Cell spreading also occurred as a threshold response but at a much higher critical concentration of sugar than for the cell-binding response. Above the critical concentration for spreading, the area occupied by a cell increased as the sugar concentration increased. By manipulating the galactose content of the matrix, cell spreading and cell binding can be differentiated as independent and separable threshold responses to the extracellular substratum.

Acrylic Resins↗
PubMed1998

The yeast galactose genetic switch is mediated by the formation of a Gal4p-Gal80p-Gal3p complex.

Saccharomyces cerevisiae responds to galactose as the sole source of carbon by activating the GAL genes encoding the enzymes of the Leloir pathway. Here, we show in vitro that the switch from repressed to activated gene expression involves the interplay of three proteins [an activator (Gal4p), a repressor (Gal80p) and an inducer (Gal3p)] and two small molecules (galactose and ATP). We also show that the galactose- and ATP-dependent interaction between Gal3p and Gal80p occurs without disruption of the Gal80p-Gal4p interaction. Thus, Gal3p-mediated activation of transcription occurs via the formation of a tripartite protein complex.

Adenosine Triphosphate↗
PubMed1997

Glucose represses the lactose-galactose regulon in Kluyveromyces lactis through a SNF1 and MIG1- dependent pathway that modulates galactokinase (GAL1) gene expression.

Expression of the lactose-galactose regulon in Kluyveromyces lactis is induced by lactose or galactose and repressed by glucose. Some components of the induction and glucose repression pathways have been identified but many remain unknown. We examined the role of the SNF1 (KlSNF1) and MIG1 (KlMIG1) genes in the induction and repression pathways. Our data show that full induction of the regulon requires SNF1; partial induction occurs in a Klsnf1 -deleted strain, indicating that a KlSNF1 -independent pathway(s) also regulates induction. MIG1 is required for full glucose repression of the regulon, but there must be a KlMIG1 -independent repression pathway also. The KlMig1 protein appears to act downstream of the KlSnf1 protein in the glucose repression pathway. Most importantly, the KlSnf1-KIMig repression pathway operates by modulating KlGAL1 expression. Regulating KlGAL1 expression in this manner enables the cell to switch the regulon off in the presence of glucose. Overall, our data show that, while the Snf1 and Mig1 proteins play similar roles in regulating the galactose regulon in Saccharomyces cerevisiae and K.lactis , the way in which these proteins are integrated into the regulatory circuits are unique to each regulon, as is the degree to which each regulon is controlled by the two proteins.

Base Sequence↗
PubMed2000

Common architecture of the primary galactose binding sites of Erythrina corallodendron lectin and heat-labile enterotoxin from Escherichia coli in relation to the binding of branched neolactohexaosylceramide.

The heat-labile enterotoxin from Escherichia coli (LT) is responsible for so-called traveller's diarrhea and is closely related to the cholera toxin (CT). Toxin binding to GM1 at the epithelial cell surface of the small intestine initiates the subsequent diarrheal disease. However, LT has a broader receptor specificity than CT in that it also binds to N-acetyllactosamine-terminated structures. The unrelated lectin from Erythrina corallodendron (ECorL) shares this latter binding property. The findings that both ECorL and porcine LT (pLT) bind to lactose as well as to neolactotetraosylceramide suggests a common structural theme in their respective primary binding sites. Superimposing the terminal galactose of the lactoses in the respective crystal structures of pLT and ECorL reveals striking structural similarities around the galactose despite the lack of sequence and folding homology, whereas the interactions of the penultimate GlcNAcb3 in the neolactotetraosylceramide differ. The binding of branched neolactohexaosylceramide to either protein reveals an enhanced affinity relative to neolactotetraosylceramide. The b3-linked branch is found to bind to the primary Gal binding pocket of both proteins, whereas the b6-linked branch outside this site provides additional interactions in accordance with the higher binding affinities found for this compound. While the remarkable architectural similarities of the primary galactose binding sites of pLT and ECorL point to a convergent evolution of these subsites, the distinguishing structural features determining the overall carbohydrate specificities are located in extended binding site regions. In pLT, Arg13 is thus found to play a crucial role in enhancing the affinity not only for N-acetyllactosamine-terminated structures but also for GM1 as compared to human LT (hLT) and CT. The physiological relevance of the binding of N-acetyllactosamine-containing glycoconjugates to LT and ECorL is briefly discussed.

Amino Sugars↗
PubMed1992

Cloning and expression of the Klebsiella pneumoniae galactose operon.

The entire galactose (gal) operon of Klebsiella pneumoniae was isolated and functionally analyzed in Escherichia coli. The genes encoding galactokinase (galK), galactose-1-phosphate uridyltransferase (galT), and UDP-galactose-4-epimerase (galE) were mapped by complementation analysis. The gene order E-T-K was found to be identical to that of Salmonella spp. and E. coli. Analysis of the nucleotide sequence in the control region revealed significant homology with that of E. coli. Two major sites for transcriptional initiation, both mapped to a cytosyl residue, were identified by primer extension. When the operon is expressed in E. coli, the K. pneumoniae gal gene products make up about 30% of the total cellular proteins. The presence of a powerful promoter responsible for high level synthesis of the gal proteins was also demonstrated using beta-galactosidase as reporter.

Amino Acid Sequence↗
PubMedDate not supplied

Identification of a galactose-like component of a chicken onco-developmental antigen.

The chemical nature of one determinant (CFA 10) of a chicken onco-developmental antigen system was investigated using both chemical modification of cell surfaces and hapten inhibition. The presence of CFA 10 on pigeon RBC's is restricted both by the developmental status of the bird and by genetic segregation within the species. The involvement of a galactose-like structure with this determinant was suggested by the ability of alpha-galactosidase, sodium-m-periodate, and galactose oxidase to destroy CFA-10 activity. Other glycosidases including beta-galactosidase and proteolytic digestion failed to alter the antigenic determinant. Sugar inhibition assays using monospecific antisera against CFA 10 verified both the galactose-like specificity of the determinant and the possible significance of an alpha- vs. beta-internal linkage. It was possible to unmask cryptic CFA-10 sites on pigeon (10-) RBC's with use of specific glycosidases. While these cryptic sites also were susceptible to alpha-galactosidase, they may not be identical to the naturally exposed CFA 10 sites on pigeon (10+) RBC's. When pigeon (10-) RBC's were incubated in vitro with serum from 10+ pigeons, CFA 10 was detectable on the RBC surface. It is suggested that one mechanism of controlling the presence of CFA 10 on pigeon RBC's may be developmental changes in gene expression mediated through the serum environment.

Animals↗
PubMed2026

Trimming galactose side chains of arabinogalactan proteins alters pectin and hemicellulose deposition in secondary cell walls of Arabidopsis thaliana floral stem internodes.

Shaping the cell wall composition and structure to meet the requirements of different tissues and developmental stages relies on multiple actors, including arabinogalactan proteins (AGPs). Although the specific role of these proteins in cell wall dynamics is still under debate, especially in events involving significant remodeling of the cell wall, their carbohydrate motif, type II arabinogalactan (AGII), seems to be crucial for their function. This study aims to investigate the function of AGII, specifically the galactose residues of its side chains, in the structural organization of the cell wall during the cessation of elongation and the transition to secondary growth. To achieve this, we characterized floral stem internodes of Arabidopsis thaliana plants overproducing the chickpea βV-galactosidase protein (35S::βV-Gal plants), an enzyme that specifically hydrolyzes the β-(1,3)- and β-(1,6)-galactosyl residues of AGII. Changes induced in the cell wall by trimming galactose residues of AGII resulted in a noticeable increase in homogalacturonan methyl esterification. Additionally, these neutral galactose side chains may regulate hemicellulose-cellulose interactions and influence xylan distribution through the cellulose network, which in turn affects the deposition of lignin and determines its recalcitrance to enzymatic degradation.

Arabidopsis↗
PubMed1985

Congenital selective malabsorption of glucose and galactose.

We review here the case histories and results of in vivo and in vitro tests for eight children with congenital selective glucose and galactose malabsorption (GGM) whom our laboratory has followed up since 1971. Clinically, GGM was manifested by intractable, acidic, sugar-containing diarrhea that started during the neonatal period. Diarrhea only abated when glucose and galactose were removed from the diet. The disease was notable for the absence of other symptoms, although mellituria was a common finding. Defective sugar transport was permanent, but sugar tolerance appeared to increase with age. In vitro, intracellular mucosal glucose concentration (C) was significantly below control level in GGM intestinal tissue for concentrations (M) of 10 and 0.1 mM glucose in the medium. C/M for galactose also decreased, while the C/M ratios for alanine and xylose were within the control range. Glucose influxes across the luminal membrane, net glucose transepithelial fluxes, and electrical parameters were all consistent with defective sodium and glucose cotransport at the brush border membrane of jejunal epithelial cells. However, the present results are also consistent with a small residual active transport system observed only at low glucose concentration in the medium. Further observations are needed to establish the role of glucose transport systems in absorption of other monosaccharides, the relationship between kidney and intestinal sodium-glucose cotransport systems, and their genetic control.

Biological Transport, Active↗
PubMed2005

GM1 ganglioside prevented the decline of hippocampal neurogenesis associated with D-galactose.

Hippocampal neurogenesis is thought to play a functional role in hippocampal-dependent learning and memory. The neurogenic capability of the hippocampus declines with age and may be associated with a decline in cognitive function. In the present study, an established model of ageing in mice was used to test the protective effects of GM1 ganglioside on hippocampal neurogenesis. This model uses D-galactose treatment to cause neuronal injury and reduced neurogenesis. GM1 significantly increased the proliferation, long-term survival and neuronal differentiation of hippocampal progenitors that had been injured with D-galactose. This study demonstrates that GM1 can protect hippocampal neurogenesis from D-galactose injury. Therefore, GM1 may protect neurogenesis in the ageing brain.

Analysis of Variance↗
PubMed1990

Activity of herpes simplex virus type 1-specified glycoprotein C antigenic site II epitopes reversibly modulated by peripheral fucose or galactose units of glycoprotein oligosaccharides.

We have previously shown that the herpes simplex virus type 1 (HSV-1)-specified glycoprotein C (gC-1) produced in epitheloid cells contains epitopes of peptide nature, which are dependent on galactose of oligosaccharides for their expression. In the present communication we report that these epitopes are expressed in a mouse neuroblastoma cell line (C1300) with low levels of galactosyl transferases. However, in place of galactose the glycoprotein from C1300 cells was found to contain oligosaccharides with additional fucose units. Fucosidase treatment, but not galactosidase treatment, abolished the antigenic activity of the carbohydrate-dependent epitopes. Altogether the results indicated that the carbohydrate-dependent epitopes of gC-1 from C1300 cells were stabilized by peripheral sugars of N-linked oligosaccharides rather than O-linked ones and that fucose could substitute for terminal galactose in promoting the activity of the carbohydrate-dependent epitopes. This is the first demonstration of the involvement of fucose in the establishment of a carbohydrate-dependent epitope of peptide nature. The results also demonstrated that reversible carbohydrate-peptide interactions were responsible for the activity of the carbohydrate-dependent epitopes.

Animals↗
PubMed1987

Uptake of galactose and lactose by Kluyveromyces lactis: biochemical characteristics and attempted genetical analysis.

Study of the lactose and galactose transport systems in Kluyveromyces lactis has shown that lactose uptake is by active transport. The transport system is under monogenic control and is inducible. Galactose uptake is also by active transport but the system is controlled by two genes which, in the four strains we studied, are present only in K. lactis CBS 2359. Galactose uptake in the other K. lactis strains is by a simple diffusion process.

Biological Transport↗
PubMed1996

Defect in export and synthesis of the periplasmic galactose receptor MglB in dnaK mutants of Escherichia coli, and decreased stability of the mglB mRNA.

The high-affinity galactose permease, which comprises the periplasmic galactose receptor MglB, the membrane translocator MglC and the membrane-associated ATPase MglA, displayed a reduced activity in a dnaK temperature-sensitive mutant of Escherichia coli. This reduced transport activity correlated with a reduction in the quantity of MglB. At 42 degrees C, an accumulation of pre-MglB in the dnaK temperature-sensitive mutant reflected a defect in MglB export. In addition, an accumulation of pre-MglB in secB, secA and secY mutants suggested that SecB and the Sec translocase are also involved in export of the periplasmic galactose receptor. At 30 degrees C, there was no accumulation of pre-MglB in the dnaK mutant, but there was still a decreased amount of MglB in the periplasm. The reduction in MglB expression was not the result of a decrease in its stability, nor was it the result of a general defect in translation or transcription, since the MglA protein (which is expressed from the same operon as MglB) was synthesized in normal amounts. Two mRNAs are implicated in the expression of the mgl genes, a polycistronic mglBAC mRNA, and a more stable and more abundant mglB mRNA, produced by 3'-5' degradation of the mglBAC mRNA (R. W. Hogg, C. Voelker & I. von Carlowitz, 1991, Mol Gen Genet 229, 453-459). The mglB mRNA is protected against exonucleases by a REP (Repetitive Extragenic Palindrome) sequence located at its 3' extremity, which is responsible for the higher expression of MglB compared to MglA and MglC. The decreased MglB expression in the dnaK mutant at 30 degrees C in the present work correlated with a reduced stability of the mglB mRNA, which may have resulted from a defective stabilization by the REP sequence, or from a defect in translation of the mglB gene.

Adenosine Triphosphatases↗
PubMed1997

Brucella abortus strain 2308 putative glucose and galactose transporter gene: cloning and characterization.

The gene for the putative transporter for glucose and galactose from Brucella abortus strain 2308 was isolated by functional complementation of Escherichia coli strains lacking either glucose or galactose transport systems. The same two plasmid clones were isolated from each screen. These clones restored glucose and galactose transport to the respective E. coli strains. The sequence of the 1806 bp overlap between these two plasmids was determined. A 1242 bp ORF whose disruption eliminated complementation of both E. coli strains showed 36% identity with the E. coli fucP gene encoding a fucose transporter. These two transporters are members of the major facilitator superfamily, in which they represent a previously undescribed family. In addition, an incomplete gene similar to E. coli hisG was found. One of the plasmids complemented E. coli hisG mutants.

Amino Acid Sequence↗
PubMed2001

Identification of a H+/glucose and galactose symporter gene glt from Xanthomonas oryzae pv. oryzae.

We identified a glucose and galactose transporter gene from the plant-pathogenic bacterium Xanthomonas oryzae pv. oryzae. Sequence analysis indicated that the gene, named glt, encoded a polypeptide of 592 amino acid residues and the product was significantly homologous with members of the Na+/glucose cotransporter (SGLT) family from mammalian and bacterial origin, especially with vSGLT from Vibrio parahaemolyticus (50% identity). GLT functioned as a glucose and galactose transporter in an Escherichia coli mutant deficient in glucose and galactose transport activity. A protonophore inhibited the transport activity, suggesting that GLT is a H+-coupled glucose/galactose symporter.

Amino Acid Sequence↗
PubMed1986

Quantitative microlocalization of diffusible ions in normal and galactose cataractous rat lens by secondary ion mass spectrometry.

Secondary ion mass spectrometry (SIMS) is a surface analytical technique with high sensitivity for elemental detection and microlocalization capabilities within the micrometre range. Quantitative analysis of epoxy resins and gelatin have been reported (Burns-Bellhorn & File, 1979). We report here the first application of this technique to quantitative microlocalization in the context of a physiological problem--analyses of sodium, potassium and calcium in normal and galactose-induced cataract in rat lens. It is known that during the development of galactose-induced cataract the whole lens content of potassium is decreased, sodium is increased and, in late stages, calcium concentration increases. Whether these alterations in diffusible ions occur homogeneously or heterogeneously is not known. Standard curves were generated from epoxy resins containing known concentrations of sodium, potassium or calcium organometallic compounds using the Cameca IMS 300 Secondary Ion Mass Spectrometer. Normal and cataractous lenses were prepared by freezing in isopentane in a liquid nitrogen bath followed by freeze-drying at -30 degrees C. After dry embedding in epoxy resin, 10 microns thick sections of lens were pressure mounted on silicon wafers, overcoated with gold, and ion emission measured under the same instrumental conditions used to obtain the standard curves. Quantitative analysis of an area 27 microns in diameter, or a total analysed volume of 1.1 microns3, was performed by using a mechanical aperture in the ion optical system. Ion images provided qualitative microanalysis with a lateral resolution of 1 micron. Control rat lenses gave values for sodium and potassium content with a precision of +/- 17% or less. These values were compared to flame photometry and atomic absorption measurements of normal lenses and were accurate within 25%. Analysis of serum and blood also gave accurate and precise measurements of these elements. Normal rat lenses had a gradient of sodium, and, to a lesser degree, of potassium from the cortex to the nucleus. Development of galactose-induced cataract was heterogeneous by morphological criteria, beginning at the lens equator and spreading from the cortex into the nucleus. However, the loss of potassium and increase in sodium concentration occurred at early stages in both the cortex and nucleus cells, possibly because these cells are interconnected by gap junctions. There is a local alteration in elemental content prior to morphologically demonstrable cataract formation.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1985

Direct and maternal aspects of the risk of cataract with partial disorders of galactose metabolism.

Partial deficiencies of the enzymes of galactose metabolism can be associated with cataract, both directly and through maternal effects during pregnancy on enzymatically normal children. However, the associations are modest, variable and not obviously expressing cause and effect. We have recorded ophthalmological and biochemical observations including oral galactose tolerance on families with established enzyme deficiencies and/or cataracts, including possible effects during pregnancy. With the partial disorders a simple relationship between the extent of biochemical abnormality and the risk of cataract is not apparent and the association may be substantially coincidental. Cataract is common, and the attractive possibility that expression is significantly due to heterozygous or lesser deficiency of the enzymes of galactose metabolism, amenable to early dietary control of children or mothers at risk, is on present evidence not well supported.

Adolescent↗