scholarly journals Properties and developmental regulation of an α-d-galactosidase from Dictyostelium discoideum

1976 ◽  
Vol 158 (2) ◽  
pp. 409-417 ◽  
Author(s):  
D C Kilpatrick ◽  
J L Stirling
Keyword(s):  
Protein Synthesis ◽  
Dictyostelium Discoideum ◽  
Early Development ◽  
Subcellular Distribution ◽  
De Novo ◽  
Specific Activity ◽  
Soluble Fraction ◽  
Developmental Regulation ◽  
Cellular Slime Mould ◽  
Cellular Slime

An alpha-D-galactosidase was detected in cells of the cellular slime mould, Dictyostelium discoideum, at all stages of development. Its specific activity was highest during early development (interphase), and this accumulation of enzyme appears to require protein synthesis de novo. Its subcellular distribution differs from that of other D. discoideum glycosidases, since most activity was recovered in the soluble fraction. No evidence was obtained for more than one isoenzymic form after subjection of extracts to electrophoresis and various chromatographic procedures. It is excreted from the cell during development, but no evidence was found for an extracellular function for the enzyme.

scholarly journals Multiple cysteine proteinase forms during the life cycle of Dictyostelium discoideum revealed by electrophoretic analysis

1988 ◽  
Vol 254 (1) ◽  
pp. 261-268 ◽  
Author(s):  
M J North ◽  
K I Scott ◽  
B C Lockwood
Keyword(s):  
Dictyostelium Discoideum ◽  
Growth And Development ◽  
Developmental Regulation ◽  
Cysteine Proteinase ◽  
Electrophoretic Analysis ◽  
Cysteine Proteinases ◽  
Cellular Slime Mould ◽  
Extracellular Form ◽  
Cellular Slime ◽  
Individual Enzyme

Proteinases of the cellular slime mould Dictyostelium discoideum have been analysed using electrophoresis on polyacrylamide gels containing gelatin (gelatin/PAGE). Multiple proteinase forms were apparent in vegetative myxamoebae, but the presence of individual enzyme forms depended on the manner in which the cells were grown. Axenic cells had a characteristic A-pattern of proteinases consisting of six bands, the most active enzymes having apparent Mr values of 51,000 and 45,000 (these have been named ddCP51 and ddCP45, respectively). Some of the proteinases were also present in the medium, the major extracellular form was ddCP42, a 42,000-Mr enzyme. Cells grown in association with bacteria had a distinct B-pattern with three main enzymes that had apparent Mr values of 48,000, 43,000 and 38,000. All of the A- and B-pattern proteinases were most active at acid pH in the presence of dithiothreitol and were inhibited by various agents such as trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E64), leupeptin and chymostatin, which inactivate cysteine proteinases. One of the enzymes, ddCP30, was identified as cysteine proteinase B which had been purified and characterized previously [North, M.J. & Whyte, A. (1984) J. Gen. Microbiol. 130, 123-134]. During starvation of axenic cells in shaken suspensions some of the vegetative proteinases disappeared, ddCP42 was released from the cells and one new enzyme with an apparent Mr of 48,000 appeared. Addition of cyclic AMP had little effect on these changes. When the axenically grown myxamoebae underwent development on filters, similar changes in band pattern were observed and the aggregation stage was characterized by the presence of three cysteine proteinase bands (apparent Mr values of 48,000, 45,000 and 43,000). Proteinases, especially ddCP42, were released from the cells and could be collected from the buffer-saturated pads which supported the filters. The results demonstrate that cysteine proteinases are present throughout growth and development of D. discoideum and that the forms present are subject to nutritional and developmental regulation.

scholarly journals Enzyme synthesis in the cellular slime mould Dictyostelium discoideum during the differentiation of myxamoebae grown axenically

1972 ◽  
Vol 126 (3) ◽  
pp. 609-615 ◽  
Author(s):  
J. Quance ◽  
J. M. Ashworth
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Cell Differentiation ◽  
Dictyostelium Discoideum ◽  
Specific Activity ◽  
Enzyme Synthesis ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Cellular Slime ◽  
Developmental Programme

1. Myxamoebae of the cellular slime mould Dictyostelium discoideum Ax-2 were grown on different media, and were harvested either in the stationary or exponential phases of the growth cycle to yield samples of myxamoebae differing in enzymic composition. 2. Morphogenesis and cell differentiation phenomena in D. discoideum appear to be similar in myxamoebae grown and harvested under different conditions. 3. The specific activity of the enzymes β-N-acetylglucosaminidase, acid phosphatase, α-mannosidase, β-glucosidase and alkaline phosphatase have been determined during cell differentiation of myxamoebae grown and harvested under different conditions. 4. The pattern of synthesis of these enzymes, all of which have been claimed to be part of the ‘developmental programme’, either remains unaffected despite the origin of the myxamoebae (alkaline phosphatase) or is qualitatively similar but quantitatively affected (acid phosphatase, β-glucosidase) or is both qualitatively and quantitatively affected by changes in the myxamoebae (α-mannosidase, β-N-acetylglucosaminidase). 5. The implications of these results for the concept of a ‘developmental programme‘ are discussed.

scholarly journals 6-Phosphogluconate dehydrogenase and the assay of uridine diphosphate glucose pyrophosphorylase in the cellular slime mould Dictyostelium discoideum

1972 ◽  
Vol 126 (3) ◽  
pp. 593-600 ◽  
Author(s):  
T. D. Edmundson ◽  
J. M. Ashworth
Keyword(s):  
Cell Differentiation ◽  
Dehydrogenase Activity ◽  
Dictyostelium Discoideum ◽  
Specific Activity ◽  
Uridine Diphosphate ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Phosphogluconate Dehydrogenase ◽  
Cellular Slime ◽  
Diphosphate Glucose

1. 6-Phosphogluconate dehydrogenase activity is present in all morphogenetic stages during cell differentiation in the cellular slime mould. 2. The different ratios of 6-phosphogluconate dehydrogenase/UDP-glucose pyrophosphorylase observed during this process can render spectrophotometric assays of UDP-glucose pyrophosphorylase inaccurate. 3. The disputed occurrence of increases in specific activity of UDP-glucose pyrophosphorylase during cell differentiation in the cellular slime mould is discussed in the light of these observations.

The Dictyostelium ribosome: biochemistry, molecular biology, and developmental regulation

1992 ◽  
Vol 70 (9) ◽  
pp. 738-750 ◽  
Author(s):  
S. Ramagopal
Keyword(s):  
Protein Synthesis ◽  
Molecular Biology ◽  
Dictyostelium Discoideum ◽  
Translational Regulation ◽  
Developmental Regulation ◽  
Cellular Slime Mold ◽  
Slime Molds ◽  
Comprehensive Review ◽  
Slime Mold Dictyostelium Discoideum ◽  
Cellular Slime

This is the first comprehensive review of ribosomes in the cellular slime mold Dictyostelium discoideum. The physicochemical, biochemical, cellular, molecular, and developmental properties are reviewed. Several features demonstrate that a unique class of ribosomes exists in this organism, and a study of these ribosomes will be important to decipher special features of translational regulation, and evolution of the organelle in the eukaryotic kingdom.Key words: cellular slime molds, development, ribosome heterogeneity, protein synthesis, evolution.

scholarly journals Adenosine 3′:5′-cyclic monophosphate-binding protein from the cellular slime mould Dictyostelium discoideum (Short Communication)

1973 ◽  
Vol 133 (3) ◽  
pp. 601-603 ◽  
Author(s):  
Al M. Malkinson ◽  
Janet Kwasniak ◽  
John M. Ashworth
Keyword(s):  
Cyclic Amp ◽  
Dictyostelium Discoideum ◽  
Short Communication ◽  
Specific Activity ◽  
Binding Protein ◽  
Protein S ◽  
Fold Increase ◽  
Axenic Medium ◽  
Cellular Slime Mould ◽  
Cellular Slime

During the differentiation of myxamoebae of Dictyostelium discoideum strain Ax-2 grown in axenic medium there is a seven- to ten-fold increase in the specific activity of cyclic AMP-binding protein(s). Evidence is presented for the belief that cyclic AMP phosphodiesterase and cyclic AMP-binding protein are distinct molecular species.

scholarly journals Growth of myxamoebae of the cellular slime mould Dictyostelium discoideum in axenic culture

1970 ◽  
Vol 119 (2) ◽  
pp. 171-174 ◽  
Author(s):  
D. J. Watts ◽  
J. M. Ashworth
Keyword(s):  
Cell Differentiation ◽  
Dictyostelium Discoideum ◽  
Axenic Culture ◽  
Axenic Medium ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Solid Media ◽  
Cellular Slime

1. A simple axenic medium suitable for the growth of the myxamoebae of a strain of the cellular slime mould Dictyostelium discoideum is described. 2. Procedures suitable for the growth of this strain in liquid and on solid media are described. 3. Conditions suitable for initiating the cell differentiation of myxamoebae grown axenically are described.

scholarly journals Glycoproteins that exhibit extensive size polymorphisms in Dictyostelium discoideum.

Genetics ◽  
1989 ◽  
Vol 122 (1) ◽  
pp. 59-64 ◽  
Author(s):  
E Smith ◽  
A A Gooley ◽  
G C Hudson ◽  
K L Williams
Keyword(s):  
Linkage Group ◽  
Dictyostelium Discoideum ◽  
Allelic Variation ◽  
Surface Glycoprotein ◽  
Developmentally Regulated ◽  
Electrophoretic Variants ◽  
Cellular Slime Mould ◽  
Repeat Units ◽  
Group I ◽  
Cellular Slime

Abstract Electrophoretic variants which arise from amino acid substitutions, leading to charge differences between proteins are ubiquitous and have been used extensively for genetic analysis. Less well documented are polymorphisms in the size of proteins. Here we report that a group of glycoproteins, which share a common carbohydrate epitope, vary in size in different isolates of the cellular slime mould, Dictyostelium discoideum. One of these proteins, PsA, a developmentally regulated prespore-specific surface glycoprotein, has previously been shown to exist in three size forms due to allelic variation at the pspA locus on linkage group I. In this report, a second glycoprotein, PsB, which is also prespore specific but found inside prespore cells, is studied. PsB maps to linkage group II and exhibits at least four different sizes in the isolates examined. We propose that the size polymorphisms are the product of allelic variation at the pspB locus, due to differences in the number of repeat units.

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