scholarly journals Phosphorylation of spore coat proteins during development of Dictyostelium discoideum

1983 ◽  
Vol 212 (3) ◽  
pp. 699-703 ◽  
Author(s):  
S J Delaney ◽  
D G Wilkinson ◽  
B D Hames
Keyword(s):  
Coat Protein ◽  
Dictyostelium Discoideum ◽  
Spore Coat ◽  
Coat Proteins ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Cellular Slime ◽  
Spore Coat Proteins ◽  
Spore Coat Protein

Immunological evidence is presented which confirms that pp95, one of the major phosphoproteins accumulated in development of the cellular slime mould Dictyostelium discoideum, is identical with spore coat protein SP13. The site of phosphorylation is identified as phosphoserine. The second major phosphorylated component, pp74, corresponds to two co-migrating spore coat proteins known collectively as SP74.

scholarly journals Incorporation of protein into spore coats is not cell autonomous in Dictyostelium.

1992 ◽  
Vol 116 (5) ◽  
pp. 1291-1300 ◽  
Author(s):  
C M West ◽  
G W Erdos
Keyword(s):  
Flow Cytometry ◽  
Coat Protein ◽  
Viscous Fluid ◽  
Fluorescent Antibody ◽  
Fluid Phase ◽  
Spore Coat ◽  
Coat Proteins ◽  
Assembly Process ◽  
Spore Coat Proteins ◽  
Spore Coat Protein

At maturity, the spores of Dictyostelium are suspended in a viscous fluid droplet, with each spore being surrounded by its own spore coat. Certain glycoproteins characteristic of the spore coat are also dissolved in this fluid matrix after the spore coat is formed. To determine whether any proteins of the coat reside in this fluid phase earlier during the process of spore coat assembly, pairs of strains which differed in a spore coat protein carbohydrate marker were mixed and allowed to form spore coats in each other's presence. We reasoned that proteins belonging to an early, soluble, extracellular pool would be incorporated into the spore coats of both strains. To detect trans-incorporation, spores were labeled with a fluorescent antibody against the carbohydrate marker and each spore's fluorescence was analyzed by flow cytometry. Several proteins of both the outer and inner protein layers of the coat appeared to be faithfully and reciprocally trans-incorporated and hence judged to belong to a soluble, assembly-phase pool. Western blot analysis of sorted spores, and EM localization, confirmed this conclusion. In contrast, one outer-layer protein was not trans-incorporated, and was concluded to be insoluble at the time of secretion. Three classes of spore coat proteins can be described: (a) Insoluble from the time of secretion; (b) present in the early, soluble pool but not the late pool after spore coat formation; and (c) present in the soluble pool throughout spore coat assembly. These classes may, respectively: (a) Nucleate spore coat assembly; (b) comprise a scaffold defining the dimensions of the nascent spore coat; and (c) complete the assembly process by intercalation into the scaffold.

Identification of a New Spore Coat Protein Gene in the Cellular Slime Mold Dictyostelium discoideum

1994 ◽  
Vol 163 (1) ◽  
pp. 49-65 ◽  
Author(s):  
Bradley K. Yoder ◽  
Jie Mao ◽  
Gregory W. Erdos ◽  
Christopher M. West ◽  
Daphne D. Blumberg
Keyword(s):  
Coat Protein ◽  
Dictyostelium Discoideum ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Slime Mold ◽  
Cellular Slime Mold ◽  
Spore Coat ◽  
Slime Mold Dictyostelium Discoideum ◽  
Cellular Slime ◽  
Spore Coat Protein

scholarly journals SpoVID Guides SafA to the Spore Coat inBacillus subtilis

2001 ◽  
Vol 183 (10) ◽  
pp. 3041-3049 ◽  
Author(s):  
Amanda J. Ozin ◽  
Craig S. Samford ◽  
Adriano O. Henriques ◽  
Charles P. Moran
Keyword(s):  
Direct Interaction ◽  
Spore Coat ◽  
Coat Proteins ◽  
Yeast Two Hybrid System ◽  
Spore Coat Proteins ◽  
Basement Layer ◽  
Two Hybrid ◽  
Spore Coat Protein

ABSTRACT Bacteria assemble complex structures by targeting proteins to specific subcellular locations. The protein coat that encasesBacillus subtilis spores is an example of a structure that requires coordinated targeting and assembly of more than 24 polypeptides. The earliest stages of coat assembly require the action of three morphogenetic proteins: SpoIVA, CotE, and SpoVID. In the first steps, a basement layer of SpoIVA forms around the surface of the forespore, guiding the subsequent positioning of a ring of CotE protein about 75 nm from the forespore surface. SpoVID localizes near the forespore membrane where it functions to maintain the integrity of the CotE ring and to anchor the nascent coat to the underlying spore structures. However, it is not known which spore coat proteins interact directly with SpoVID. In this study we examined the interaction between SpoVID and another spore coat protein, SafA, in vivo using the yeast two-hybrid system and in vitro. We found evidence that SpoVID and SafA directly interact and that SafA interacts with itself. Immunofluorescence microscopy showed that SafA localized around the forespore early during coat assembly and that this localization of SafA was dependent on SpoVID. Moreover, targeting of SafA to the forespore was also dependent on SpoIVA, as was targeting of SpoVID to the forespore. We suggest that the localization of SafA to the spore coat requires direct interaction with SpoVID.

Cloning and expression of a cDNA that comprises part of the gene coding for a spore coat protein of Dictyostelium discoideum

1984 ◽  
Vol 4 (11) ◽  
pp. 2273-2278
Author(s):  
B C Dowds ◽  
W F Loomis
Keyword(s):  
Dictyostelium Discoideum ◽  
Cdna Clone ◽  
Single Gene ◽  
Polyclonal Antiserum ◽  
Cloning And Expression ◽  
Spore Coat ◽  
Coat Proteins ◽  
Developmentally Regulated ◽  
Gene Coding ◽  
Spore Coat Proteins

The three major spore coat proteins of Dictyostelium discoideum are developmentally regulated, cell-type-specific proteins. They are packaged in prespore vesicles and then secreted to form the outer layer of spore coats. We have isolated a cDNA clone from the gene coding for one of these proteins, SP96, a glycoprotein of 96,000 daltons. We screened the cDNA bank by the method of hybrid select translation followed by immunoprecipitation of the translation products with SP96-specific polyclonal antiserum. We found that the gene was first transcribed into stable mRNA a few hours before the time of detection of SP96 synthesis and that the mRNA, like the protein, accumulated specifically in prespore cells and spores. SP96 constituted the same proportion of newly synthesized protein as the proportion of its message in polyadenylated RNA. SP96 appeared to be encoded by a single gene as judged by Southern blot analysis of digested genomic DNA hybridized to the cDNA clone.

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.

Control of cellular differentiation by temperature in the cellular slime mould Dictyostelium discoideum

1984 ◽  
Vol 69 (1) ◽  
pp. 159-165
Author(s):  
M. Maeda
Keyword(s):  
Low Temperature ◽  
Dictyostelium Discoideum ◽  
Cellular Differentiation ◽  
Cellular Slime Mould ◽  
Slime Mould ◽  
Cellular Slime

The effects of low temperature on morphogenesis and cellular differentiation of Dictyostelium discoideum were examined. During incubation at 5 degrees C, the vegetative and preaggregation cells never developed, but cell masses at the aggregation or slug stage developed to form hemispherical, or dumbbell-shaped multicellular structures. By staining with FITC-antispore IgG, the structures formed after 10 days of incubation of tipped aggregates at 5 degrees C were found to be composed of 90% spores, 5% prespore cells and 5% non-stained cells. Since only 20% of the total cells constituting the tipped aggregate had been prespore cells at the beginning of incubation, this showed that spore differentiation proceeded even at low temperature, while stalk differentiation was completely inhibited. Similar results were obtained when the cells were incubated at 3 degrees C. However, at 0 degree C, morphogenesis and cellular differentiation did not occur, although most of the prespore cells at the late culmination stage differentiated incompletely into spores. Possible reasons for the high proportion of spores being induced by low temperature are discussed.

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