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PubMed2004

Characterization of a glycosylphosphatidylinositol-bound cell-wall protein (GPI-CWP) in Yarrowia lipolytica.

The structure and composition of the cell wall of yeast has so far been studied mainly in Saccharomyces cerevisiae. It is basically made up of three components: beta-glucans, chitin and mannose-containing glycoproteins, also called mannoproteins. Most covalently bound cell-wall mannoproteins belong to the so-called glycosylphosphatidylinositol cell-wall protein (GPI-CWP) family, cell-wall proteins that are bound through the remnant of a GPI residue to 1,6-beta-glucan. The non-conventional yeast Yarrowia lipolytica shares Generally Regarded As Safe (GRAS) status with S. cerevisiae, has some industrial applications and is increasingly being proposed as a host for the production of recombinant proteins and as a model in the study of dimorphism. However, very little information on cell-wall structure and composition is available for this organism. Here is described the isolation and characterization of YlCWP1, a homologue of the CWP1 gene from S. cerevisiae, which encodes a GPI-CWP, and the identification of its gene product. YlCWP1 encodes a 221 aa protein that contains a putative signal peptide and a putative GPI-attachment site. It shows 28.5 % overall identity with Cwp1 of S. cerevisiae and a hydropathy profile characteristic of GPI-CWPs. Disruption of YlCWP1, both in the wild-type and in an mnn9 glycosylation-deficient background, led to the identification of Ylcwp1 as a 60 kDa polypeptide present in cell-wall extracts. To the authors' knowledge, this is the first report of a GPI-CWP in Y. lipolytica, and it suggests that the cell-wall organization of Y. lipolytica is similar to that of S. cerevisiae.

Amino Acid Sequence↗
PubMed1977

Cell wall carbohydrates in Phycomyces blakeslesanus Burgeff.

The carbohydrate composition of the cell walls from spores, mycelium and sporangiophores of Phycomyces blakesleeanus was analyzed. Spore wall polysaccharides contained over 50% glucose, about 20% uronic acids, 10% mannose and 10% amino-sugars. During the growth of the hyphae amino-sugars became the main carbohydrate (45%); uronic acids contributed some 25%, glucose and fructose 10% and galactose nearly 6%. Sporangiophores contained almost 90% aminosurgars and some 6% uronic acids. Traces of rhamnose were found in all wall preparations. A similar picture emerged from studies on the incorporation of [U-14C]-glucose into wall materials. Furthermore we looked for a GDP-fucose synthesizing system and found an increasing activity during early germination. This rise in activity was inhibited by cycloheximide but only by 5-fluorouracil.

Amino Sugars↗
PubMed1987

Ultrastructure and biochemistry of the cell wall of Methanococcus voltae.

The ultrastructure and chemical composition of the cell wall of the marine archaebacterium Methanococcus voltae were studied by negative-staining and freeze-etch electron microscopy and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. M. voltae possesses a single regularly structured (RS) protein layer external to the plasma membrane. Freeze-etch preparations of cells indicated that the protein subunits are hexagonally arranged with a center-to-center spacing of approximately 10 nm. The extracted RS protein had a molecular weight of 76,000. It was present on envelopes prepared by shearing in a French press, osmotic lysis, or sonication, as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. NaCl was not required for attachment of the RS protein to the underlying plasma membrane. The hexagonal array could be demonstrated by platinum shadowing and freeze-etching of envelopes, but negative staining in the abscence of NaCl failed to stabilize the array. The RS protein could be solubilized by urea, guanidine hydrochloride, dithiothreitol, and several detergents, including Nonidet P-40, Triton X-100, and Tween 20. However, the most specific release of the wall protein from envelopes occurred after a heat treatment in HEPES (N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid) buffer at 50 to 60 degrees C.

Bacterial Proteins↗
PubMed2000

Bacterial cell wall-induced arthritis: chemical composition and tissue distribution of four Lactobacillus strains.

To study what determines the arthritogenicity of bacterial cell walls, cell wall-induced arthritis in the rat was applied, using four strains of Lactobacillus. Three of the strains used proved to induce chronic arthritis in the rat; all were Lactobacillus casei. The cell wall of Lactobacillus fermentum did not induce chronic arthritis. All arthritogenic bacterial cell walls had the same peptidoglycan structure, whereas that of L. fermentum was different. Likewise, all arthritogenic cell walls were resistant to lysozyme degradation, whereas the L. fermentum cell wall was lysozyme sensitive. Muramic acid was observed in the liver, spleen, and lymph nodes in considerably larger amounts after injection of an arthritogenic L. casei cell wall than following injection of a nonarthritogenic L. fermentum cell wall. The L. casei cell wall also persisted in the tissues longer than the L. fermentum cell wall. The present results, taken together with those published previously, underline the possibility that the chemical structure of peptidoglycan is important in determining the arthritogenicity of the bacterial cell wall.

Animals↗
PubMed1967

Effect of growth rate and substrate limitation on the composition and structure of the cell wall of Saccharomyces cerevisiae.

1. A study was made of the composition and structure of walls isolated from yeast grown in continuous culture at different rates, under three conditions of glucose limitation in which the concentrations of glucose and ammonium sulphate in the medium and the oxygen-transfer rate in the culture were varied, and one condition of NH(4) (+) limitation. 2. The contents of total glucan and total mannan in the walls were relatively little affected by the growth rate under any of the four sets of conditions. The phosphorus and protein contents of walls from yeast grown under each of the four conditions increased as the growth rate was decreased. Walls from yeast grown under NH(4) (+) limitation contained only half as much protein as walls from cells grown under glucose limitation. The proportion of lipid was greatest in walls from yeast grown under NH(4) (+) limitation. 3. A procedure was devised for fractionating isolated walls, based on the ease with which the glucan and mannan were extracted with water and with hot and cold 6% (w/v) potassium hydroxide solution. The percentage of glucan, mannan, protein and phosphorus in each of the fractions was affected by the rate of growth and by the nature of the substrate limitation. 4. The beta-fructofuranosidase activities of yeast grown under glucose limitation increased as the growth rate was lowered, but decreased at very low growth rates. The effects at low growth rates were probably due to repression of enzyme synthesis by residual glucose in the culture filtrate. The beta-fructofuranosidase activities of yeast grown under NH(4) (+) limitation were much lower than those from yeast grown under any of the conditions of glucose limitation. 5. Yeast cells grown at any of the rates under NH(4) (+) limitation were longer and thinner than those grown at the same rate under any of the conditions of glucose limitation. Mean cell volumes were dependent on growth rate but not on the nature of the substrate limitation. 6. Electron micrographs of thin sections of isolated walls showed that cells grown under NH(4) (+) limitation had a more porous structure than those from cells grown under any of the conditions of glucose limitation.

Cell Wall↗
PubMed2000

Yeast cell attachment: a tool modulating wall composition and resistance to 5-bromo-6-azauracil.

The attachment of Candida utilis, Kluyveromyces lactis, and Saccharomyces cerevisiae cells stimulates an increase in the content of cell wall polysaccharides and mannoproteins, accompanied by increased resistance to the inhibitory effect of 5-bromo-6-azauracil. The covalent attachment of viable yeasts was accomplished (via dialdehyde-amino spacers) by reaction of aldehyde groups of the carrier with reactive amino groups in accessible cell surface proteins. The employed technique enables the optimization of yeast sources of beta-1,3-, beta-1,6- glucans, mannan, and mannoprotein. The modulatory effect of the cell attachment is discussed.

Journal Article↗
PubMed1998

The S-layer proteins of two Bacillus stearothermophilus wild-type strains are bound via their N-terminal region to a secondary cell wall polymer of identical chemical composition.

Two Bacillus stearothermophilus wild-type strains were investigated regarding a common recognition and binding mechanism between the S-layer protein and the underlying cell envelope layer. The S-layer protein from B. stearothermophilus PV72/p6 has a molecular weight of 130,000 and assembles into a hexagonally ordered lattice. The S-layer from B. stearothermophilus ATCC 12980 shows oblique lattice symmetry and is composed of subunits with a molecular weight of 122,000. Immunoblotting, peptide mapping, N-terminal sequencing of the whole S-layer protein from B. stearothermophilus ATCC 12980 and of proteolytic cleavage fragments, and comparison with the S-layer protein from B. stearothermophilus PV72/p6 revealed that the two S-layer proteins have identical N-terminal regions but no other extended structurally homologous domains. In contrast to the heterogeneity observed for the S-layer proteins, the secondary cell wall polymer isolated from peptidoglycan-containing sacculi of the different strains showed identical chemical compositions and comparable molecular weights. The S-layer proteins could bind and recrystallize into the appropriate lattice type on native peptidoglycan-containing sacculi from both organisms but not on those extracted with hydrofluoric acid, leading to peptidoglycan of the A1gamma chemotype. Affinity studies showed that only proteolytic cleavage fragments possessing the complete N terminus of the mature S-layer proteins recognized native peptidoglycan-containing sacculi as binding sites or could associate with the isolated secondary cell wall polymer, while proteolytic cleavage fragments missing the N-terminal region remained unbound. From the results obtained in this study, it can be concluded that S-layer proteins from B. stearothermophilus wild-type strains possess an identical N-terminal region which is responsible for anchoring the S-layer subunits to a secondary cell wall polymer of identical chemical composition.

Amino Acid Sequence↗
PubMed1989

Chemical composition of Eubacterium alactolyticum cell wall peptidoglycan.

The mechanism of lysis of Eubacterium alactolyticum cell walls by Streptomyces albus G enzyme was studied. The analysis of the peptide terminal groups and peptide subunits isolated from the cell wall digest, released during solubilization of the cell walls, revealed that lytic action of S. albus G enzyme was mainly due to D-alanyl-A2pm endopeptidase, N-acetylmuramyl-L-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase. E. alactolyticum cell wall peptidoglycan is composed mainly of glucosamine, muramic acid, D-glutamic acid, L- and D-alanine, meso-diaminopimelic acid and glycine. The peptide subunit consists of L-alanyl-D-glutamyl-meso-A2pm-D-alanine. D-Alanine is connected directly with the amino group of the meso-A2pm residue of another peptide subunit. All of the L-amino groups of meso-diaminopimelic acid are involved in cross-linking. The possible structure of the peptide moiety of E. alactolyticum cell wall peptidoglycan is presented.

Amino Acids↗
PubMed1989

Chemical composition of Eubacterium nodatum cell wall peptidoglycan.

The structure of Eubacterium nodatum cell wall peptidoglycan was investigated. The peptide subunit of E. nodatum peptidoglycan has the following structure: L-Ala-D-Glu (Gly)-L-Orn-D-Ala. The carboxyl group of alanine occupying position 4 is attached to the delta-amino group of ornithine of an other subunit by the cross-linking bridge L-Ala-L-Ala-L-Orn. All glycine molecules are connected with the alpha-carboxyl group of glutamic acid with the ratio being 0.5-1. The hydrolysis of E. nodatum peptidoglycan by the S. albus G enzyme proceeds primarily due to the activity of alanyl-alanine endopeptidase, ornithyl-ornithine endopeptidase, ornithyl-alanine endopeptidase, N-acetyl-muramyl-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase.

Amino Acids↗
PubMed1983

Chemical composition and structure of cell wall teichoic acids of staphylococci.

The cell wall teichoic acid structures of 22 staphylococci including 13 type strains were determined. Most of the strains contain a poly(polyolphosphate) teichoic acid with glycerol and/or ribitol as polyol component. The polyolphosphate backbone is partially substituted with various combinations of sugars and/or amino sugars. Most of the substituents occur in a monomeric form but some strains also contain dimers of N-acetylglucosamine as substituents. Staphylococcus hyicus subsp. hyicus NCTC 10350 and S. sciuri DSM 20352 revealed rather complex cell wall teichoic acids. They consist of repeating sequences of phosphate-glycerol-phosphate-N-acetylglucosamine. The amino sugar component is present in this case as a monomer or an oligomer (n less than or equal to 3). Moreover, the glycerol residues are partially substituted with N-acetylglucosamine. The cell wall teichoic acid of S. auricularis is a poly(N-acetylglucosaminyl-phosphate) polymer similar to that found in S. caseolyticus ATCC29750. The cell wall teichoic acid structures for type strains of S. auricularis, S. capitis, S. cohnii, S. haemolyticus, S. hominis, S. hyicus subsp. hyicus, S. sciuri, S. xylosus and S. warneri were determined for the first time in detail. The structures of some of the previously described teichoic acids had to be revised (S. epidermidis, S. simulans, S. aureus phage type 187).

Acetylglucosamine↗
PubMed1970

The enzymic composition of the isolated cell wall and plasma membrane of baker's yeast.

A study was made of the enzyme content of the isolated cell walls and of a plasma-membrane preparation obtained by centrifugation after enzymic digestion of the cell walls of baker's yeast. The isolated cell walls showed no hexokinase, alkaline phosphatase, esterase or NADH oxidase activity. It was concluded that these enzymes exist only in the interior of the cell. Further, only a negligible activity of deamidase was detectable in the cell walls. Noticeable amounts of saccharase, phosphatases hydrolysing p-nitrophenyl phosphate, ATP, ADP, thiamin pyrophosphate and PP(i), with optimum activity at pH3-4, and an activity of Mg(2+)-dependent adenosine triphosphatase at neutral pH, were found in the isolated cell walls. During enzymic digestion, the other activities appearing in the cell walls were mostly released into the medium, but the bulk of the Mg(2+)-dependent adenosine triphosphatase remained in the plasma-membrane preparation. Accordingly, it may be assumed that the enzymes released into the medium during digestion are located in the cell wall outside the plasma membrane, whereas the Mg(2+)-dependent adenosine triphosphatase is an enzyme of the plasma membrane. This enzyme differs from the phosphatases with pH optima in the range pH3-4 with regard to location, pH optimum, substrate specificity and different requirement of activators.

Adenine Nucleotides↗
PubMed1970

The effect of ethylenediaminetetra-acetate on Pseudomonas alcaligenes and the composition of the bacterial cell wall.

1. EDTA in borate buffer has a marked bactericidal effect on Pseudomonas alcaligenes, which is more sensitive than Pseudomonas aeruginosa. The bactericidal effect is accompanied by solubilization of lipopolysaccharide and release of intracellular solutes. These effects are more pronounced at pH9.2 than 7.1. 2. Cell walls of P. alcaligenes were prepared and from them were obtained the readily extracted lipids and the fractions given by treatment with aqueous phenol. 3. The cell walls and the above components were analysed and results are compared with those for P. aeruginosa. 4. Lipopolysaccharide obtained by treatment of cell walls with aqueous phenol is contaminated with glycosaminopeptide to a variable extent. 5. The lipopolysaccharide contains less neutral sugar but more phosphorus than the lipopolysaccharide of P. aeruginosa; fucosamine is not a component of the lipopolysaccharide of P. alcaligenes.

Amino Acids↗