QUALITATIVE ANALYSES OF VEGETATIVE CELL WALLS AND SPORE WALLS OF SOME REPRESENTATIVE SPECIES OF STREPTOMYCES

1966 ◽  
Vol 12 (5) ◽  
pp. 985-994 ◽  
Author(s):  
Peter J. DeJong ◽  
Elizabeth McCoy
Keyword(s):  
Cell Wall ◽  
Aspartic Acid ◽  
Vegetative Cell ◽  
Cell Walls ◽  
Teichoic Acid ◽  
Minor Component ◽  
Paper Electrophoresis ◽  
Diaminopimelic Acid ◽  
Streptomyces Species ◽  
Spore Walls

Vegetative cell walls and spore walls of seven Streptomyces species representing four types of spore morphology were qualitatively analysed for their components. Amino acid and carbohydrate components (glucose, glucosamine, muramic acid, diaminopimelic acid, glutamic acid, glycine, alanine, arginine, threonine, valine, leucine, and aspartic acid) in both types of walls were identical in all species. Aspartic acid was a major component in spore walls, but a minor component in vegetative cell walls. Although organic phosphate was present in both vegetative- and spore-wall hydrolysates, the other components of teichoic acid were not found nor was teichoic acid extracted from the isolated walls by cold trichloroacetic acid. A portion of the vegetative cell wall was rendered soluble with lysozyme and separated by paper electrophoresis into two fractions detected with ninhydrin. The lysozyme-resistant portion of the vegetative cell wall showed the same major and minor components as the spore walls, which are also lysozyme resistant.

scholarly journals Autolysis of cell walls of Bacillus stearothermophilus B65 and the chemical structure of the peptidoglycan

1970 ◽  
Vol 118 (5) ◽  
pp. 859-868 ◽  
Author(s):  
W. D. Grant ◽  
A. J. Wicken
Keyword(s):  
Glutamic Acid ◽  
Cell Walls ◽  
Bacillus Stearothermophilus ◽  
Teichoic Acid ◽  
Paper Electrophoresis ◽  
Diaminopimelic Acid ◽  
Peptide Fragments ◽  
Acid Complex ◽  
Acid Hydrolysate ◽  
Peptide Mixture

1. The cell walls of Bacillus stearothermophilus B65 contain glucosamine, muramic acid, alanine, α∈-diaminopimelic acid (Dap), glutamic acid, aspartic acid, glycine, and serine in the molecular proportions 0.60:0.64:2.30:0.85:1.00:0.11:0.13:0.31. 2. Both d- and l-alanine are present, but glutamic acid and diaminopimelic acid are present only as the d- and meso-isomers respectively. 3. The peptide fragments Ala-Dap, Dap-Ala, and Dap-Ala-Dap have been isolated from a partial acid hydrolysate of the cell walls. 4. The major products of autolysis of the cell wall were d-alanine, a peptide mixture, peptidoglycan material and a peptidoglycan–teichoic acid complex. 5. Separation of the peptide mixture into ten major peptides was achieved by DEAE-Sephadex and paper chromatography, and paper electrophoresis. 6. The structures of these peptides have been determined and they fall into four groups, the individual members of each group differing only in number or position of carboxamide substituents. 7. The structures are I, a tripeptide l-Ala–d-Glu-meso-Dap; II, a pentapeptide made up by the tripeptide (I) linked through the ∈-amino group of its diaminopimelic acid residue to the carboxyterminal of the dipeptide meso-Dap-d-Ala; III, a heptapeptide made up by a similar linkage between the tripeptide (I) and the tetrapeptide l-Ala-d-Glu-meso-Dap-d-Ala; IV, a possible undecapeptide made up by a further tetrapeptide similarly linked to the heptapeptide (III) structure. 8. The structure of the peptidoglycan and the actions of the autolytic enzymes are discussed in terms of these peptide structures.

scholarly journals Die Aminosäuresequenz des Serin und Asparaginsäure enthaltenden Mureins von Bifidobacterium bifidum Orla Jensen/ The amino acid sequence of the serin and aspartic acid containing mureins of Bifidobacterium bifidum ORLA JENSEN

1970 ◽  
Vol 25 (11) ◽  
pp. 1294-1301 ◽  
Author(s):  
Dieter Koch ◽  
Karl Heinz Schleifer ◽  
Otto Kandler
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Cell Walls ◽  
Teichoic Acid ◽  
Bifidobacterium Bifidum ◽  
Muramic Acid ◽  
Partial Acid Hydrolysis

Cell walls of Bifidobacterium bifidum var. pennsylvanicus were isolated. The polysaccharide consisted of glucose, galactose and rhamnose. Teichoic acid was not present. The murein (peptidoglycan) contained MurNAc, GlcNH2NAc, ᴅ-Glu, Ala. ʟ-Ser, ᴅ-Asp and L-Orn in a ratio of about 1 : 1 : 1 : 2 : 1 : 1 : 1. In one batch a high amount of ʟ-glutamic acid was found. It was not a constituent of the murein since it remained in the lysozyme insensitive residue.The amino acid sequence of the murein was determined by analyzing the oligopeptides arising during partial acid hydrolysis. It was shown that the peptide subunits attached to the muramic acid are the same as in many other mureins: ʟ-Ala-ᴅ-Glu-ʟ-Orn-D-Ala. The interpeptide bridge consisted of β-ᴅ-aspartyl-ʟ-serine. Since about 35% of aspartic acid and 6% of ornithine are N-terminal in the cell wall, it was assumed that only 60% of the peptide subunits are cross-linked. 4 other strains of B. bifidum proved to contain the same type of murein. While all other strains of other species of Bifidobacterium investigated contained other types of murein, it seems likely that the Orn-Ser-Asp type of the murein is typical of B. bifidum.

scholarly journals The extraction of cell walls of Pseudomonas aeruginosa with aqueous phenol. The insoluble residue and material from the aqueous layers

1967 ◽  
Vol 105 (2) ◽  
pp. 759-765 ◽  
Author(s):  
K. Clarke ◽  
G. W. Gray ◽  
D. A. Reaveley
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Wall ◽  
Cell Walls ◽  
Lipid A ◽  
Diaminopimelic Acid ◽  
Insoluble Residue ◽  
Muramic Acid ◽  
Gram Negative ◽  
Gram Negative Organisms ◽  
Residue Fraction

1. The insoluble residue and material present in the aqueous layers resulting from treatment of cell walls of Pseudomonas aeruginosa with aqueous phenol were examined. 2. The products (fractions AqI and AqII) isolated from the aqueous layers from the first and second extractions respectively account for approx. 25% and 12% of the cell wall and consist of both lipopolysaccharide and muropeptide. 3. The lipid part of the lipopolysaccharide is qualitatively similar to the corresponding material (lipid A) from other Gram-negative organisms, as is the polysaccharide part. 4. The insoluble residue (fraction R) contains sacculi, which also occur in fraction AqII. On hydrolysis, the sacculi yield glucosamine, muramic acid, alanine, glutamic acid and 2,6-diaminopimelic acid, together with small amounts of lysine, and they are therefore similar to the murein sacculi of other Gram-negative organisms. Fraction R also contains substantial amounts of protein, which differs from that obtained from the phenol layer. 5. The possible association or aggregation of lipopolysaccharide, murein and murein sacculi is discussed.

scholarly journals Pectin Rhamnogalacturonan II: On the “Small Stem with Four Branches” in the Primary Cell Walls of Plants

2011 ◽  
Vol 2011 ◽  
pp. 1-11 ◽  
Author(s):  
Beda M. Yapo
Keyword(s):  
Cell Wall ◽  
Cell Walls ◽  
Vascular Plants ◽  
Minor Component ◽  
Primary Cell ◽  
Side Chains ◽  
Complex Cell ◽  
Rhamnogalacturonan Ii ◽  
Branching Point ◽  
A Chain

Rhamnogalacturonan II (RG-II) is a type of block copolymer of complex pectins that represents a quantitatively minor component of the primary cell walls of land (vascular) plants. The structural composition of RG-II is almost totally sequenced and appears to be remarkably conserved in all tracheophytes so far examined. The backbone of RG-II, released from complex (cell wall) pectins by endo-polygalacturonase (Endo-PG) treatment, has been found to contain up to 15 (1→4)-linked-α-D-GalpA units, some of which carry four well-defined side chains, often referred to as A-, B-, C-, and D-side chains. Nevertheless, the relative locations on the backbone of these four branches, especially the A chain, remain to be ascertained. A combination of different data suggests that neither the terminal nonreducing GalA nor the contiguous GalA unit is likely to be the branching point of the A chain, but probably the ninth GalA residue from the reducing end, assuming a minimum backbone length of 11 (1→4)-linked-α-d-GalpA. The latest reports on RG-II are here highlighted, with a provided update for the macrostructure and array of functionalities.

scholarly journals The configuration of 2,6-diamino-3-hydroxypimelic acid in microbial cell walls

1969 ◽  
Vol 115 (4) ◽  
pp. 797-805 ◽  
Author(s):  
H R Perkins
Keyword(s):  
Cell Wall ◽  
Hydroxy Group ◽  
Cell Walls ◽  
Optical Rotation ◽  
Periodate Oxidation ◽  
Ring Closure ◽  
Diaminopimelic Acid ◽  
Amino Group ◽  
Amino Groups ◽  
Peptide Linkage

β-Hydroxydiaminopimelic acid, together with some diaminopimelic acid, occurs in the cell-wall mucopeptide of certain Actinomycetales. These components were converted into their di-DNP derivatives and separated by chromatography. Hence the relative proportions present in the cell walls of a number of species were measured. The problem of acid-induced inversion of configuration was studied. Of the diaminohydroxypimelic acids isomer B (see Scheme 2; amino groups meso, hydroxy group threo to its neighbouring amino group) always predominated but a small proportion of isomer D (amino groups l, hydroxy group erythro) also occurred. The configuration of the diaminohydroxypimelic acids was determined by periodate oxidation to glutamic γ-semialdehyde, which underwent spontaneous ring-closure. Reduction with sodium borohydride produced optically active proline, the configuration of which was determined by direct measurement of the optical rotation of DNP-proline. Un-cross-linked diaminohydroxypimelic acid in the cell wall was oxidized with periodate in the presence of ammonia. Since the remaining amino group was bound in peptide linkage, ring-closure was prevented and borohydride reduction of the aldehyde–ammonia presumed to be present resulted in the formation of ornithine. The quantity of ornithine was used as a measure of the degree of cross-linking.

scholarly journals Structural studies of a mannitol teichoic acid from the cell wall of bacterium N.C.T.C. 9742

1985 ◽  
Vol 226 (2) ◽  
pp. 587-599 ◽  
Author(s):  
W J Anderton ◽  
S G Wilkinson
Keyword(s):  
Cell Wall ◽  
Hydroxy Group ◽  
Alkaline Hydrolysis ◽  
Teichoic Acid ◽  
Paper Electrophoresis ◽  
Spectroscopic Studies ◽  
Exchange Chromatography ◽  
Brevibacterium Linens ◽  
Brevibacterium Epidermis ◽  
Hydrolysis Of

Degradative and n.m.r.-spectroscopic studies have been carried out on a novel mannitol teichoic acid extracted from the cell wall of bacterium N.C.T.C. 9742, for which the name Brevibacterium iodinum has been proposed. The backbone of the polymer is a poly(D-mannitol phosphate) containing 1--6 phosphodiester linkages. In most residues, pyruvic acid is acetal-linked to positions 4 and 5 of the mannitol. About half of the mannitol residues carry a beta-D-glucopyranosyl substituent at position 2. The glucosylmannitol was isolated and thoroughly characterized. At least 24 products were detected by ion-exchange chromatography and paper electrophoresis after alkaline hydrolysis of the polymer. Not all of these products could be identified. The main mechanistic pathways for depolymerization by the cleavage of phosphodiester linkages during alkaline hydrolysis involved (a) participation by the 2-hydroxy group and a cyclic phosphodiester intermediate (leading to a series of mannitol-based products) and (b) participation by the 3-hydroxy group in the cyclization of mannitol (leading to a series of products based on 1,4-anhydromannitol). The presence of glycerol phosphates in hydrolysates could be ascribed either to a linkage unit or to a separate glycerol teichoic acid. The mannitol teichoic acid was absent from the cell walls of Brevibacterium linens and Brevibacterium epidermis (one strain of each was examined).

Die gemeinsame Wurzel der Lyse von Escherichia coli durch Penicillin oder durch Phagen

1957 ◽  
Vol 12 (7) ◽  
pp. 421-427 ◽  
Author(s):  
W. Weidel ◽  
J. Primosigh
Keyword(s):  
Cell Wall ◽  
Cell Walls ◽  
Building Blocks ◽  
Diaminopimelic Acid ◽  
Wall Structure ◽  
Gram Positive ◽  
E Coli ◽  
Growing Cell ◽  
Cell Wall Disruption ◽  
Entire Cell

One of the two layers of the E. coli B cell wall is shown to possess the chemical composition typical of a gram-positive microorganism. It is this layer which lends support and strength to the entire cell wall structure, its rigidity depending up on the incorporation of building blocks made up from alanine, glutamic acid, diaminopimelic acid, muramic acid and glucosamine.Phage enzyme is an agent capable of removing these stabilizing units from the „gram-positive “ layer, thereby causing it to collapse. Penicillin appears to prevent the biosynthetic incorporation of the same stabilizing units into growing cell walls, thus producing eventually the effect of cell wall disruption in a basically similar way.The rather manifold aspects of these findings are discussed at some length.

scholarly journals CHEMICAL BASIS FOR AN IMMUNOLOGICAL SPECIFICITY OF A STRAIN OF STAPHYLOCOCCUS AUREUS

1963 ◽  
Vol 117 (6) ◽  
pp. 925-935 ◽  
Author(s):  
William G. Juergens ◽  
Arnold R. Sanderson ◽  
Jack L. Strominger
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Degradation Product ◽  
Cell Walls ◽  
Horse Serum ◽  
Teichoic Acid ◽  
Aureus Strain ◽  
Chemical Basis ◽  
Immunological Specificity ◽  
Group A

Antisera, prepared against formalin-killed cells of Staphylococcus aureus, strain Copenhagen, agglutinated the cell walls of this strain. The agglutination was inhibited by the teichoic acid from the cell wall of this strain, by any degradation product of this teichoic acid which contained the α-acetylglucosaminyl-ribitol unit, by α-phenyl-acetylglucosaminide, and by N-acetylglucosamine, but not by a large number of other haptens related to the cell wall. In quantitative experiments, however, only 40 to 50 per cent of antibody adsorption to cell wall could be inhibited by teichoic acid or by N-acetylglucosamine. The α-acetylglucosaminyl-ribitol unit in the teichoic acid is, therefore, an important immunological determinant in the cell wall of this strain, although other immunological specificities may also exist. The cell walls were also agglutinated by heterologous antisera prepared against streptococcal Group A carbohydrate or against horse serum azophenyl-ß-acetylglucosaminide. The heterologous agglutination, however, was specific for the ß-acetylglucosaminyl-ribitol units in the teichoic acid.

scholarly journals Cell-wall thickening in Bacillus subtilis. Comparison of thickened and normal walls

1970 ◽  
Vol 120 (1) ◽  
pp. 159-170 ◽  
Author(s):  
R. C. Hughes ◽  
P. J. Tanner ◽  
Elaine Stokes
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Walls ◽  
Teichoic Acid ◽  
Cellular Growth ◽  
Wall Thickening ◽  
Complete Medium ◽  
Bacillus Subtilis 168 ◽  
Normal Wall

1. Incubation of Bacillus subtilis 168 trp in a glucose–amino acids–salts medium lacking tryptophan leads to an inhibition of cellular growth without affecting cell-wall synthesis. The cell walls increased approximately two- to three-fold in thickness and at the same time the amount of mucopeptide in the cells measured chemically increased to about the same extent. 2. Synthesis of mucopeptide and teichoic acid as measured by the extent of incorporation of radioactivity continued linearly for approximately 1h and then stopped. No reason was found for the strictly limited synthesis of the wall polymers. 3. The initial rates of incorporation of [32P]Pi or [3H]alanine into teichoic acid and of 3H-labelled amino acids into mucopeptide were not appreciably inhibited by the addition of chloramphenicol to the glucose–amino acids–salts medium. 4. There was no selective turnover of the mucopeptide synthesized by the cells in a medium lacking tryptophan on resumption of growth in a complete medium. 5. Wall synthesis taking place during the thickening process was similar to normal wall synthesis proceeding in growing cells. Walls of different thicknesses prepared from cells incubated for various times in incomplete medium did not differ qualitatively in composition. The products of autolysis of thickened walls were isolated and the analyses indicated a close similarity in the details of their mucopeptide structure compared with the mucopeptide of cells growing in the exponential phase.

Sign in / Sign up

Export Citation Format

Share Document