scholarly journals Characterization of a Major Bacillus anthracis Spore Coat Protein and Its Role in Spore Inactivation

2004 ◽  
Vol 186 (8) ◽  
pp. 2413-2417 ◽  
Author(s):  
Ho-San Kim ◽  
D. Sherman ◽  
F. Johnson ◽  
A. I. Aronson
Keyword(s):  
Coat Protein ◽  
Bacillus Anthracis ◽  
Spore Coat ◽  
Wild Type ◽  
Gene Encoding ◽  
Promising Target ◽  
Section Electron ◽  
Group A ◽  
Dark Staining ◽  
Spore Coat Protein

ABSTRACT A major Bacillus anthracis spore coat protein of 13.4 kDa, designated Cotα, was found only in the Bacillus cereus group. A stable ca. 30-kDa dimer of this protein was also present in spore coat extracts. Cotα, which is encoded by a monocistronic gene, was first detected late in sporulation, consistent with a σK-regulated gene. On the basis of immunogold labeling, the protein is in the outer spore coat and absent from the exosporium. In addition, disruption of the gene encoding Cotα resulted in spores lacking a dark-staining outer spore coat in thin-section electron micrographs. The mutant spores were stable upon heating or storage, germinated at the same rate as the wild type, and were resistant to lysozyme. They were, however, more sensitive than the wild type to phenol, chloroform, and hypochlorite but more resistant to diethylpyrocarbonate. In all cases, resistance or sensitivity to these reagents was restored by introducing a clone of the cotα gene into the mutant. Since Cotα is an abundant outer spore coat protein of the B. cereus group with a prominent role in spore resistance and sensitivity, it is a promising target for the inactivation of B. anthracis spores.

scholarly journals CotA of Bacillus subtilis Is a Copper-Dependent Laccase

2001 ◽  
Vol 183 (18) ◽  
pp. 5426-5430 ◽  
Author(s):  
Marie-Françoise Hullo ◽  
Ivan Moszer ◽  
Antoine Danchin ◽  
Isabelle Martin-Verstraete
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Uv Light ◽  
Specific Substrate ◽  
Spore Coat ◽  
Wild Type ◽  
Multicopper Oxidases ◽  
Spore Pigment ◽  
Spore Coat Protein

ABSTRACT The spore coat protein CotA of Bacillus subtilisdisplays similarities with multicopper oxidases, including manganese oxidases and laccases. B. subtilis is able to oxidize manganese, but neither CotA nor other sporulation proteins are involved. We demonstrate that CotA is a laccase. Syringaldazine, a specific substrate of laccases, reacted with wild-type spores but not with ΔcotA spores. CotA may participate in the biosynthesis of the brown spore pigment, which appears to be a melanin-like product and to protect against UV light.

Developmental expression and characterization of the gene encoding spore coat protein SP60 in Dictyostelium discoideum

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
Keyword(s):  
Coat Protein ◽  
Dictyostelium Discoideum ◽  
Developmental Expression ◽  
Spore Coat ◽  
Gene Encoding ◽  
Spore Coat Protein

The Promoter of a Gene Encoding a Novel Dictyostelium Spore Coat Protein

1994 ◽  
Vol 163 (1) ◽  
pp. 38-48 ◽  
Author(s):  
Bradley K. Yoder ◽  
Daphne D. Blumberg
Keyword(s):  
Coat Protein ◽  
Spore Coat ◽  
Gene Encoding ◽  
Spore Coat Protein

scholarly journals Localization of the Transglutaminase Cross-Linking Sites in the Bacillus subtilis Spore Coat Protein GerQ

2006 ◽  
Vol 188 (21) ◽  
pp. 7609-7616 ◽  
Author(s):  
Alicia Monroe ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Cross Linking ◽  
Spore Coat ◽  
Bacillus Subtilis Spore ◽  
Binding Partners ◽  
Lysine Residues ◽  
Cross Links ◽  
Hydrolysis Of ◽  
Spore Coat Protein

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.

Expression, Localization and Modification of YxeE Spore Coat Protein in Bacillus subtilis

2007 ◽  
Vol 142 (6) ◽  
pp. 681-689 ◽  
Author(s):  
R. Kuwana ◽  
H. Takamatsu ◽  
K. Watabe
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Spore Coat ◽  
Spore Coat Protein

scholarly journals Characterization, purification and synthesis of spore-coat protein in Bacillus megaterium KM

1982 ◽  
Vol 202 (1) ◽  
pp. 231-241 ◽  
Author(s):  
G S A B Stewart ◽  
D J Ellar
Keyword(s):  
Coat Protein ◽  
Bacillus Megaterium ◽  
Early Stage ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Stage Iv ◽  
Spore Coat ◽  
Methionine Residue ◽  
Protein Incorporation ◽  
Spore Coat Protein

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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