Immunoelectron Microscopic Studies on Spore Coat Proteins of <i>Bacillus megaterium</i>

Imagawa, Masayoshi; Ohtsuka, Mikiko; Nakatani, Yoshihiro; Oku, Yuichi; El‐Belbasi, Hussein I.; Nishihara, Tsutomu; Kondo, Masaomi

doi:10.1111/j.1348-0421.1988.tb01463.x

Cited by 3 publications

(2 citation statements)

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“…Collectively, these analyses indicate that the B. megaterium QM B1551 spore coat and exosporium are comprised and assembled from a substantially different subset of proteins to their orthologous Bacillus counterparts. Several biochemical‐led studies aimed at characterising the B. megaterium QM B1551 spore coat were published through the 1970s to early 1990s (Imagawa et al ., , ; Nishihara et al ., ; Takubo et al ., ). Unfortunately, these studies predated the availability of virtually any B. megaterium genomic information and tools for targeted genetic manipulation.…”

Section: Introductionmentioning

confidence: 99%

BMQ_0737 encodes a novel protein crucial to the integrity of the outermost layers ofBacillus megateriumQM B1551 spores

Manetsberger

Hall

Christie

2014

FEMS Microbiol Lett

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Bioinformatic and electron microscopy analyses indicate that the composition of the B. megaterium QM B1551 spore coat is likely to differ substantially from other Bacillus species. We report here on the identification and characterisation of novel B. megaterium proteins that appear to be abundant in the spore coat. All three proteins, encoded by loci BMQ_0737, BMQ_3035 and BMQ_4051, were identified by proteomic analysis of alkaline detergent extracts from mature spores. Putative spore coat proteins were characterised by transcriptional, reporter-fusion and mutagenesis analyses supported by fluorescence and transmission electron microscopy. These analyses revealed that BMQ_0737 is a novel morphogenetic protein that is required for the correct assembly of the B. megaterium outer spore coat and exosporium, both of which are structurally compromised or missing in BMQ_0737 null mutant spores.

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Section: Introductionmentioning

confidence: 99%

BMQ_0737 encodes a novel protein crucial to the integrity of the outermost layers ofBacillus megateriumQM B1551 spores

Manetsberger

Hall

Christie

2014

FEMS Microbiol Lett

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“…It was concluded that three proteins (P48, P36, and P22) absent in the mature spores of the OL deficient mutants are the components of OL, since they were found in SDS/DTT-soluble proteins of the higher density band. Recently, Imagawa et al (10) reported that P48 antigen was found only in the OL region from immunoelectron microscopic studies.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Deposition of the Proteins in the Outermost Layer of Bacillus megaterium Spore

Takubo

Okuda

Takemura

et al. 1989

Microbiology and Immunology

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It was proved that three spore coat proteins of 48, 36, and 22 kDa (P48, P36, and P22) were the components of the outermost layer (OL) of Bacillus megaterium ATCC 12872 spore by analysis of the isolated OL. And it was indicated that these proteins were deposited not by disulfide bond, but by ionic and/or hydrophobic bonds on the spore. Among them, P36 and P22 were expected to be located on the very surface of the spore by immunological analysis. In the OL deficient mutant of B. megaterium ATCC 12872, MAE05, whose spore was lacking in these OL proteins and galactosamine-6-phosphate polymer, both P36 and P22 were present in the mother cell cytoplasm and deposited on the forespores, but they disappeared with the lysis of mother cells. An OL protein-releasing factor having proteolytic activity was detected in the culture supernatant at the late sporulating stage of both the wild-type and the mutant strains. But the factor could not act on the proteins of the mature spores and the forespores at tin (tn indicates n hr after the end of exponential growth) of the wild-type strain. Moreover, P36 and P22 were found in the spores of a revertant of MAE05 which could form galactosamine-6-phosphate polymer, suggesting that this sugar polymer played the role in protecting the OL proteins against the protease-like substance after the deposition.

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Biochemical defects of outermost layer deficient mutants during sporulation of Bacillus megaterium

Takubo

Inoue²,

Kunimatsu³

et al. 1992

Can. J. Microbiol.

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To determine the regulation of morphogenesis of the outermost layer, the thick layer outside the inner coat, of the Bacillus megaterium spore, we isolated 15 outermost layer deficient mutants of B. megaterium using transposon Tn917. Three mutant strains lacked both synthesis of the 48-kDa outermost layer protein and induction of two initial enzymes for galactosamine-6-phosphate polymer synthesis, evidence that these biochemical events are regulated in the cascade system during morphogenesis of the outermost layer.

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Immunoelectron Microscopic Studies on Spore Coat Proteins of Bacillus megaterium

Abstract: An immunochemical staining technique for the spore coat proteins of

Cited by 3 publications

References 14 publications

BMQ_0737 encodes a novel protein crucial to the integrity of the outermost layers ofBacillus megateriumQM B1551 spores

BMQ_0737 encodes a novel protein crucial to the integrity of the outermost layers ofBacillus megateriumQM B1551 spores

Characterization and Deposition of the Proteins in the Outermost Layer of Bacillus megaterium Spore

Biochemical defects of outermost layer deficient mutants during sporulation of Bacillus megaterium

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