Biomaterial Database

Mutants of Dictyostelium discoideum blocked in expression of all members of the developmentally regulated discoidin multigene family. 1983

S Alexander, and T M Shinnick, and R A Lerner

Mutant strains of D. discoideum are described that can complete morphogenesis and cytodifferentiation but which express vastly reduced levels of the galactose-binding lectins discoidin I and II (less than 1% and 1%-2% respectively) compared to the wild-type control. Mutant cells proceeding through development lack lectin activity, lectin protein, and specific lectin mRNA. In contrast, the genes encoding these proteins are present in their wild-type configurations in the genome. Since these proteins are encoded by four to five discrete genes, the mutations in these strains are most likely in genes involved in the regulation of the expression of members of this multigene family. The results also indicate that the discoidin lectins may not be required for fruiting body construction in this organism. Finally, coupled with the recent ability to transform D. discoideum, these mutants open the way to identification and isolation of regulatory genes and their products.

UI	MeSH Term	Description	Entries
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D002454	Cell Differentiation	Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.	Differentiation, Cell,Cell Differentiations,Differentiations, Cell
D004023	Dictyostelium	A genus of protozoa, formerly also considered a fungus. Its natural habitat is decaying forest leaves, where it feeds on bacteria. D. discoideum is the best-known species and is widely used in biomedical research.	Dictyostelium discoideum,Dictyostelium discoideums,Dictyosteliums,discoideum, Dictyostelium
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005656	Fungal Proteins	Proteins found in any species of fungus.	Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D005786	Gene Expression Regulation	Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.	Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D000070821	Discoidins	Lectins that were identified in DICTYOSTELIUM DISCOIDEUM. They bind to GALACTOSE and are involved in cell-substratum adhesion, maintenance of morphology during aggregation, and spore formation.	Discoidin,Discoidin-I,Discoidin-II,Discoidin I,Discoidin II
D015800	Protozoan Proteins	Proteins found in any species of protozoan.	Proteins, Protozoan
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal
D037161	Galectins	A class of animal lectins that bind specifically to beta-galactoside in a calcium-independent manner. Members of this class are distiguished from other lectins by the presence of a conserved carbohydrate recognition domain. The majority of proteins in this class bind to sugar molecules in a sulfhydryl-dependent manner and are often referred to as S-type lectins, however this property is not required for membership in this class.	Galaptins,Lectins, S-Type,D-Galactoside-Binding Lectin,Galactose-Binding Lectin,Galectin,S-Type Lectin,S-Type Lectins,beta-D-Gal(1-3)D-GalNAc Specific Lectins,beta-D-Galactosyl-Specific Lectin,beta-Galactoside Binding Lectin,Binding Lectin, beta-Galactoside,D Galactoside Binding Lectin,Galactose Binding Lectin,Lectin, D-Galactoside-Binding,Lectin, Galactose-Binding,Lectin, S-Type,Lectin, beta-D-Galactosyl-Specific,Lectin, beta-Galactoside Binding,Lectins, S Type,S Type Lectin,S Type Lectins,beta D Galactosyl Specific Lectin,beta Galactoside Binding Lectin