Search results for "Chitin Synthase"
showing 10 items of 13 documents
Sedimentation properties of chitosomal chitin synthetase from the wild-type strain and the 'slime' variant of Neurospora crassa.
1989
Marked differences in the pattern of sedimentation of cellular structures were observed after isopycnic centrifugation of crude cell-free preparations from the Neurospora crassa wall-less 'slime' variant and mycelial wild-type strain. Kinetic studies of particle sedimentation showed that the various types of subcellular components, as revealed by turbidity, UV absorption, polypeptide patterns, and chitin synthetase activity determinations, sediment independently of one another. An important feature was the finding that chitin synthetase from 'slime' peaked at a median specific gravity of 1.1201 +/- 0.0036, whereas that from wild-type strain sedimented at a higher buoyant density (specific g…
Chitin synthetase activity in Candida albicans: subcellular distribution in yeast cells and protoplasts
1991
Chitin synthetase activity was detected in a partly zymogenic form in cell-free homogenates obtained from C. albicans yeast cells and protoplasts of the same type of cells. By isopycnic centrifugation on sucrose gradients of the cell-free homogenates two fractions with chitin synthetase activity were obtained: one was associated with the plasma membrane (labelled with [ 3 H]concanavalin A (con A) and buoyant density 1·195 g ml −1 ) in a partly active state, and the second was in the cytoplasm, where the enzyme was in a particulate fully zymogenic form, lacking affinity to con A. The buoyant density of the enzyme found in this location depended on the method of cell breakage. Lysis of partly…
Stability of chitin synthetase in cell-free preparations of a wild-type strain and a 'slime' variant of Neurospora crassa.
1991
Chitin synthetase activity in cell-free preparations from a wild-type strain and a 'slime' variant of Neurospora crassa was monitored over many days in samples stored at 0 degrees C. Total activity in whole-cell-free extracts and low-speed supernatants from both organisms was very unstable, losing more than 90% of the initial activity on storage at 0 degrees C for 96 h. Chitin synthetase detection was not masked by chitinase activity present in the preparations. Gel-filtration chromatography of these preparations increased the stability of the activity from the 'slime' variant, whereas removal of particulate structures by high-speed centrifugation stabilized the chitin synthetase activity i…
Loss of virulence in Ustilago maydis by Umchs6 gene disruption
2003
A gene encoding a sixth chitin synthase (Umchs6, sequence GenBank accession No. AF030554) from the plant pathogenic hemibasidiomycete Ustilago maydis (DC.) Cda. was isolated and characterized. The predicted protein is 1103 amino acids in length with a calculated molecular mass of 123.5 kDa. a2b2 null mutants were obtained by substitution of a central fragment of the Umchs6 gene with the hygromycin resistance cassette, and a1b1 null mutants were obtained by genetic recombination in plants of an a2b2Δch6 and a wild-type a1b1 strain. The mutation had no effect on the dimorphic transition in vitro or on mating, and growth rate of the mutants was only slightly reduced. On the other hand, they di…
Regulation of chitin synthase activity inSaccharomyces cerevisiae: Effect of the inhibition of cell division and of synthesis of RNA and protein
1980
The effect of pronase and trypsin on the activation or deactivation (degradation?) of chitin synthase ofSaccharomyces cerevisiae occurs faster in membranous preparations than in toluene-treated cells. When the temperature is raised, the former preparation is deactivated earlier than the latter one. The activity found in growing cells is not modified after inhibition of protein synthesis by cycloheximide or amino acid starvation or by the inhibition of RNA synthesis. It was possible to activate the chitin synthase ofS. cerevisiae cdc 25 grown at 23°C by means of pronase, whereas trypsin had no effect. After the cells were grown at 37°C, chitin synthase could not be activated either with tryp…
Synthesis and Assembly of Wall Polymers on Regenerating Yeast Protoplasts
1983
Accumulation of chitin and glucan on S. cerevisiae and C. albicans protoplasts begins shortly after resuspension in the regeneration medium, and mannoprotein molecules also appear retained by the regenerating wall after 30–60 minutes in S. cerevisiae or after a longer lag period in C. albicans. Nevertheless, a considerable fraction of the synthesized mannoproteins, which in SDS-acrylamide gels exhibit a different pattern from that of wall mannoproteins of cells, are still released to the growth medium during at least eight hours. De novo synthesis of chitin synthase, but not of glucan synthase, is observed in S. cerevisiae from about 30 minutes after initiation of the regeneration process. …
Chitin: A Structural Biopolysaccharide
2009
Chitin is a naturally occurring fibre-forming polymer that plays a protective role in many lower eukaryotes similar to that of cellulose in plants. Chemically it is a long-chain unbranched polysaccharide made of N-acetylglucosamine residues; it is the second most abundant organic compound in nature, after cellulose. Taking into account the structural role played by chitin, its metabolism (synthesis and degradation) is essential for different morphogenetic events. Absent in vertebrates and plants, chitin represents a parasite-specific target for chemotherapeutic attack and also plays a role in host immune responses. Because of its abundance in nature and its properties, biotechnological appl…
Evidence for the involvement of acylglycerides on chitin synthetase activity inCandida albicans
1991
The effect of a lipase activity (EC 3.1.1.3) on the chitin synthetase from Candida albicans has been studied, both on the active and the trypsin activated enzyme. Removal of fatty acids from acylglycerides by lipase has an inhibitory effect on the activity as well as on the ‘in vitro’ activation process by trypsin in the membrane-bound enzyme and in the chitosomes. This would indicate that an adequate lipid environment is required for both the activation process and proper function of the synthetase activity.
Separation of chitosomal chitin synthetase from cell-free extracts ofNeurospora crassa “Slime” variant agglutinated with concanavalin A
1989
Cell-free extracts of the wall-less slime variant ofNeurospora crassa were treated with concanavalin A (Con A); this treatment caused a massive agglutination of the particulate structures in the cell-free homogenate, although most (73%) of the chitin synthetase initially present in the cell-free extract remained in the supernatant obtained after sedimentation of the lectin-flocculated material. This chitin synthetase showed the sedimentation properties of chitosomes (unique microvesicular structures) and failed to bind [3H]Con A. A significant percentage (42%) of the chitin synthetase activity associated with the Con A-flocculated material probably corresponds to mechanically trapped chitos…
Chitin: A Structural Biopolysaccharide with Multiple Applications
2014
Chitin is a naturally occurring fibre-forming polymer that plays a protective role in many lower eukaryotes similar to that of cellulose in plants. Chemically it is a long-chain unbranched polysaccharide made of N-acetylglucosamine residues linked through β-1,4 covalent bonds; it is the second most abundant organic compound in nature, after cellulose. Taking into account the role played by chitin in different biological structures (i.e. fungal cell walls, insect peritrophic matrix, insect and crustacean cuticles, eggshells from nematodes, cyst wall of protozoa), its metabolism (biosynthesis and degradation) is essential for different morphogenetic events. Absent in vertebrates and plants, c…