Isolation and characterization of spore coat protein (sp96) gene of Dictyostelium discoideum

1990 ◽  
Vol 31 (1) ◽  
pp. 1-9 ◽  
Author(s):  
M. Tasaka ◽  
M. Hasegawa ◽  
T. Ozaki ◽  
M. Iwabuchi ◽  
I. Takeuchi
1990 ◽  
Vol 4 (6) ◽  
pp. 951-960 ◽  
Author(s):  
D. C. C Widdowson ◽  
J. A. Proffitt ◽  
P. S. Jagger ◽  
A. J. Richards ◽  
B. D. Hames

2006 ◽  
Vol 72 (1) ◽  
pp. 972-975 ◽  
Author(s):  
Shin-ichi Sakasegawa ◽  
Hidehiko Ishikawa ◽  
Shigeyuki Imamura ◽  
Haruhiko Sakuraba ◽  
Shuichiro Goda ◽  
...  

ABSTRACT The spore coat protein CotA from Bacillus subtilis was previously identified as a laccase. We have now found that CotA also shows strong bilirubin oxidase activity and markedly higher affinity for bilirubin than conventional bilirubin oxidase. This is the first characterization of bilirubin oxidase activity in a bacterial protein.


1991 ◽  
Vol 100 (2) ◽  
pp. 357-364
Author(s):  
F. P. GIBSON ◽  
T. SCHOFIELD ◽  
B. D. HAMES

Spore coat protein synthesis in submerged pseudoplasmodia of Dictyostelium discoideum is dependent on the presence of a low relative molecular mass extracellular factor, SPIF, the activity of which can be mimicked by methionine. In vitro translation and northern blot analysis revealed that the level of spore coat protein mRNA in pseudoplasmodia incubated in the absence of methionine is little different from that in its presence. Furthermore, nogalamycin, a potent inhibitor of RNA synthesis, does not prevent the regulation of spore coat protein synthesis by methionine. These data suggest that the regulatory step is probably at the translational level. The proportion of total ribosomes associated in polysomes in pseudoplasmodia incubated in the absence of methionine is substantially lower than in its presence indicating a relative decrease in the number of translationally active mRNAs. However, measurements of the average polysome size and ribosome transit time in pseudoplasmodia initiated in the presence or absence of methionine show that the initiation rate of protein synthesis is essentially identical in both situations.


1994 ◽  
Vol 163 (1) ◽  
pp. 49-65 ◽  
Author(s):  
Bradley K. Yoder ◽  
Jie Mao ◽  
Gregory W. Erdos ◽  
Christopher M. West ◽  
Daphne D. Blumberg

1983 ◽  
Vol 212 (3) ◽  
pp. 699-703 ◽  
Author(s):  
S J Delaney ◽  
D G Wilkinson ◽  
B D Hames

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.


2006 ◽  
Vol 188 (21) ◽  
pp. 7609-7616 ◽  
Author(s):  
Alicia Monroe ◽  
Peter Setlow

ABSTRACT The Bacillus subtilis spore coat protein GerQ is necessary for the proper localization of CwlJ, an enzyme important in the hydrolysis of the peptidoglycan cortex during spore germination. GerQ is cross-linked into high-molecular-mass complexes in the spore coat late in sporulation, and this cross-linking is largely due to a transglutaminase. This enzyme forms an ε-(γ-glutamyl) lysine isopeptide bond between a lysine donor from one protein and a glutamine acceptor from another protein. In the current work, we have identified the residues in GerQ that are essential for transglutaminase-mediated cross-linking. We show that GerQ is a lysine donor and that any one of three lysine residues near the amino terminus of the protein (K2, K4, or K5) is necessary to form cross-links with binding partners in the spore coat. This leads to the conclusion that all Tgl-dependent GerQ cross-linking takes place via these three lysine residues. However, while the presence of any of these three lysine residues is essential for GerQ cross-linking, they are not essential for the function of GerQ in CwlJ localization.


2007 ◽  
Vol 142 (6) ◽  
pp. 681-689 ◽  
Author(s):  
R. Kuwana ◽  
H. Takamatsu ◽  
K. Watabe

1982 ◽  
Vol 202 (1) ◽  
pp. 231-241 ◽  
Author(s):  
G S A B Stewart ◽  
D J Ellar

The spore-coat fraction from Bacillus megaterium KM, when prepared by extraction of lysozyme-digested integuments with SDS (sodium dodecyl sulphate) and urea, contains three N-terminal residues and a major component of apparent mol.wt. 17500. Electron microscopy of this fraction shows it to consist of an ordered multilamellar structure similar to that which forms the coat region of intact spores. The 17500-dalton protein, which has been purified to homogeneity, has an N-terminal methionine residue, has high contents of glycine, proline, cysteine and acidic amino acids and readily polymerized even in the presence of thiol-reducing agents. It is first synthesized between late Stage IV and early Stage V, which correlates with the morphological appearance of spore coat. Before Stage VI the 17500-dalton protein is extractable from sporangia by SDS in the absence of thiol-reducing reagents. Between Stage VI and release of mature spores the protein becomes resistant to extraction by SDS unless it is supplemented by a thiol-reducing reagent. In addition to that of the spore-coat protein, the timing of synthesis of all the integument proteins was analysed by SDS/polyacrylamide-gel electrophoresis and non-equilibrium pH-gradient electrophoresis. Several integument proteins are conservatively synthesized from as early as 1h after the end of exponential growth (t1), which may reflect protein incorporation into the spore outer membrane.


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