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.

scholarly journals Transglutaminase-Mediated Cross-Linking of GerQ in the Coats of Bacillus subtilis Spores

2004 ◽  
Vol 186 (17) ◽  
pp. 5567-5575 ◽  
Author(s):  
Katerina Ragkousi ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Molecular Mass ◽  
High Molecular Mass ◽  
Cross Linking ◽  
Spore Coat ◽  
Coat Proteins ◽  
Formation Pathway ◽  
Mutant Strains ◽  
Hydrolysis Of ◽  
Spore Coat Protein

ABSTRACT The spores of Bacillus subtilis show remarkable resistance to many environmental stresses, due in part to the presence of an outer proteinaceous structure known as the spore coat. GerQ is a spore coat protein essential for the presence of CwlJ, an enzyme involved in the hydrolysis of the cortex during spore germination, in the spore coat. Here we show that GerQ is cross-linked into higher-molecular-mass forms due in large part to a transglutaminase. GerQ is the only substrate for this transglutaminase identified to date. In addition, we show that cross-linking of GerQ into high-molecular-mass forms occurs only very late in sporulation, after mother cell lysis. These findings, as well as studies of GerQ cross-linking in mutant strains where spore coat assembly is perturbed, lead us to suggest that coat proteins must assemble first and that their cross-linking follows as a final step in the spore coat formation pathway.

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 Temporal and spatial regulation of protein cross-linking by the pre-assembled substrates of a Bacillus subtilis spore coat transglutaminase

PLoS Genetics ◽  
2019 ◽  
Vol 15 (4) ◽  
pp. e1007912 ◽  
Author(s):  
Catarina G. Fernandes ◽  
Diogo Martins ◽  
Guillem Hernandez ◽  
Ana L. Sousa ◽  
Carolina Freitas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cross Linking ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Spatial Regulation ◽  
Bacillus Subtilis Spore ◽  
Temporal And Spatial ◽  
Protein Cross Linking

Diffraction pattern of Bacillus subtilis CotY spore coat protein 2D crystals

2021 ◽  
Vol 197 ◽  
pp. 111425
Author(s):  
Michal Bodík ◽  
Daniela Krajčíková ◽  
Jakub Hagara ◽  
Eva Majkova ◽  
Imrich Barák ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Diffraction Pattern ◽  
Spore Coat ◽  
2D Crystals ◽  
Spore Coat Protein

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.

scholarly journals Bilirubin Oxidase Activity of Bacillus subtilis CotA

2006 ◽  
Vol 72 (1) ◽  
pp. 972-975 ◽  
Author(s):  
Shin-ichi Sakasegawa ◽  
Hidehiko Ishikawa ◽  
Shigeyuki Imamura ◽  
Haruhiko Sakuraba ◽  
Shuichiro Goda ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Oxidase Activity ◽  
Spore Coat ◽  
Bacterial Protein ◽  
Bilirubin Oxidase ◽  
Spore Coat Protein

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.

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