scholarly journals Alternative Translation Initiation Produces a Short Form of a Spore Coat Protein in Bacillus subtilis

2001 ◽  
Vol 183 (6) ◽  
pp. 2032-2040 ◽  
Author(s):  
Amanda J. Ozin ◽  
Teresa Costa ◽  
Adriano O. Henriques ◽  
Charles P. Moran
Keyword(s):  
Bacillus Subtilis ◽  
Translation Initiation ◽  
Stop Codon ◽  
Short Form ◽  
Mature Spore ◽  
Multilayered Structure ◽  
Full Length ◽  
Spore Coat ◽  
Single Transcript ◽  
Spore Coat Protein

ABSTRACT During endospore formation in Bacillus subtilis,over two dozen polypeptides are localized to the developing spore and coordinately assembled into a thick multilayered structure called the spore coat. Assembly of the coat is initiated by the expression of morphogenetic proteins SpoIVA, CotE, and SpoVID. These morphogenetic proteins appear to guide the assembly of other proteins into the spore coat. For example, SpoVID forms a complex with the SafA protein, which is incorporated into the coat during the early stages of development. At least two forms of SafA are found in the mature spore coat: a full-length form and a shorter form (SafA-C30) that begins with a methionine encoded by codon 164 of safA. In this study, we present evidence that the expression of SafA-C30arises from translation initiation at codon 164. We found only a single transcript driving expression of SafA. A stop codon engineered just upstream of a predicted ribosome-binding site near codon M164 abolished formation of full-length SafA, but not SafA-C30. The same effect was observed with an alanine substitution at codon 1 of SafA. Accumulation of SafA-C30 was blocked by substitution of an alanine codon at codon 164, but not by a substitution at a nearby methionine at codon 161. We found that overproduction of SafA-C30 interfered with the activation of late mother cell-specific transcription and caused a strong sporulation block.

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

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.

Examination of the function of two kelch proteins generated by stop codon suppression

Development ◽  
1997 ◽  
Vol 124 (7) ◽  
pp. 1405-1417 ◽  
Author(s):  
D.N. Robinson ◽  
L. Cooley
Keyword(s):  
Stop Codon ◽  
Full Length ◽  
Open Reading Frames ◽  
Female Sterility ◽  
Ring Canal ◽  
Ring Canals ◽  
Specific Manner ◽  
Single Transcript ◽  
Reading Frames ◽  
Canal Morphology

The Drosophila kelch gene produces a single transcript with a UGA stop codon separating two open reading frames (ORF1 and ORF2). From the transcript, 76 kDa ORF1 and 160 kDa full-length (ORF1 + ORF2) proteins are made. The expression of these two proteins is regulated in a tissue-specific manner causing the ratio of full-length to ORF1 protein to vary in different tissues. The only detected defect for kelch mutants is female sterility, and kelch protein is localized to the ovarian ring canals. kelch mutant ring canals are disorganized and have partly occluded lumens, causing a failure to transport cytoplasm. ORF1 and full-length kelch proteins co-sediment with ring canals suggesting that both proteins are found in the ring canals. Transgenetic analysis reveals that ORF1 kelch protein is sufficient to rescue ring canal morphology and fertility. In addition, we have mutated the UGA stop codon to a UAA stop codon and to three sense codons that allow constitutive readthrough. Analysis of these mutants reveals that a full-length kelch protein can partially compensate for the loss of endogenous kelch, but the residue included at the stop codon is critical for function. Finally, these studies suggest that the mechanism of stop codon suppression of kelch is by tRNA suppression.

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.

scholarly journals Relation between uptake of glycine and biosynthesis of spore coat protein during sporulation of Bacillus subtilis.

1980 ◽  
Vol 44 (1) ◽  
pp. 17-24
Author(s):  
Takahiko MITANI ◽  
Eiichi NOZAWA ◽  
Kinichi SUGAE ◽  
Kozo ASANO ◽  
Hajime KASOTA
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Spore Coat ◽  
Spore Coat Protein
Sign in / Sign up

Export Citation Format

Share Document