Transglutaminase in sporulating cells of Bacillus subtilis.

Kobayashi, Katsunori; Suzuki, Shunichi; Izawa, Yuko; Yokozeki, Kenzo; Miwa, Kiyoshi; Yamanaka, Shigeru

doi:10.2323/jgam.44.85

Cited by 47 publications

(35 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Transglutaminase activity was detected late during sporulation and in spores of B. subtilis as well as in sporulating cells of other Bacillus species (16,18,37). An inspection of the regulatory region of the tgl gene of B. subtilis has revealed sequences similar to those utilized by the K form of RNA polymerase as well as possible GerE-binding sites and has led to the suggestion that tgl transcription could require both K and GerE (16).…”

Section: Expression Of Tglmentioning

confidence: 99%

See 1 more Smart Citation

Assembly and Function of a Spore Coat-Associated Transglutaminase of Bacillus subtilis

et al. 2005

View full text Add to dashboard Cite

The assembly of a multiprotein coat around the Bacillus subtilis spore confers resistance to lytic enzymes and noxious chemicals and ensures normal germination. Part of the coat is cross-linked and resistant to solubilization. The coat contains -(␥-glutamyl)lysyl cross-links, and the expression of the gene (tgl) for a sporeassociated transglutaminase was shown before to be required for the cross-linking of coat protein GerQ. Here, we have investigated the assembly and function of Tgl. We found that Tgl associates, albeit at somewhat reduced levels, with the coats of mutants that are unable to assemble the outer coat (cotE), that are missing the inner coat and with a greatly altered outer coat (gerE), or that are lacking discernible inner and outer coat structures (cotE gerE double mutant). This suggests that Tgl is present at various levels within the coat lattice. The assembly of Tgl occurs independently of its own activity, as a single amino acid substitution of a cysteine to an alanine (C116A) at the active site of Tgl does not affect its accumulation or assembly. However, like a tgl insertional mutation, the tglC116A allele causes increased extractability of polypeptides of about 40, 28, and 16 kDa in addition to GerQ (20 kDa) and affects the structural integrity of the coat. We show that most Tgl is assembled onto the spore surface soon after its synthesis in the mother cell under K control but that the complete insolubilization of at least two of the Tgl-controlled polypeptides occurs several hours later. We also show that a multicopy allele of tgl causes increased assembly of Tgl and affects the assembly, structure, and functional properties of the coat.

show abstract

Section: Expression Of Tglmentioning

confidence: 99%

“…In contrast, a transglutaminase activity is detected in sporulating cells and spores (16,18,37), and ε-(␥-glutamyl)lysyl cross-links have been detected in B. subtilis spores and in purified coat material (17). Moreover, the gene (tgl) for a transglutaminase was cloned following the purification of a spore-associated activity (16,37).…”

mentioning

confidence: 99%

Assembly and Function of a Spore Coat-Associated Transglutaminase of Bacillus subtilis

et al. 2005

View full text Add to dashboard Cite

show abstract

“…The B. subtilis spore coat is composed of several distinct layers and contains Ն30 proteins, almost all of which are spore-specific gene products (5)(6)(7)(8)(9)(10)(11)(12). There is extensive cross-linking of a number of proteins in the coats, at least in part by a transglutaminase and perhaps by the formation of dityrosine cross-links as well (13)(14)(15)(16)(17)(18).…”

mentioning

confidence: 99%

The Bacillus subtilis spore coat provides “eat resistance” during phagocytic predation by the protozoan Tetrahymena thermophila

Klobutcher

Ragkousi

Setlow

2005

Proc. Natl. Acad. Sci. U.S.A.

121

124

View full text Add to dashboard Cite

Bacillus spores are highly resistant to many environmental stresses, owing in part to the presence of multiple ''extracellular'' layers. Although the role of some of these extracellular layers in resistance to particular stresses is known, the function of one of the outermost layers, the spore coat, is not completely understood. This study sought to determine whether the spore coat plays a role in resistance to predation by the ciliated protozoan Tetrahymena, which uses phagocytosis to ingest and degrade other microorganisms. Wild-type dormant spores of Bacillus subtilis were efficiently ingested by the protozoan Tetrahymena thermophila but were neither digested nor killed. However, spores with various coat defects were killed and digested, leaving only an outer shell termed a rind, and supporting the growth of Tetrahymena. A similar rind was generated when coat-defective spores were treated with lysozyme alone. The sensitivity of spores with different coat defects to predation by T. thermophila paralleled the spores' sensitivities to lysozyme. Spore killing by T. thermophila was by means of lytic enzymes within the protozoal phagosome, not by initial spore germination followed by killing. These findings suggest that a major function of the coat of spores of Bacillus species is to protect spores against predation. We also found that indigestible rinds were generated even from spores in which cross-linking of coat proteins was greatly reduced, implying the existence of a coat structure that is highly resistant to degradative enzymes.Bacillus spore ͉ phagocytosis ͉ spore resistance

show abstract

“…Among them, TGase from guinea pig liver and human blood coagulation factor XIIIa have been well studied and characterized (Folk & Chung, 1973). Because of the advantage of mass production, many researchers (Ando et al, 1989;Ramanujam & Hageman, 1990;Klein et al,1992;Kobayashi et al, 1998) have performed screening of microorganisms producing TGase. Ando et al (1989) first found that some Streptoverticillium (S.) sp.…”

mentioning

confidence: 99%

Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

Umezawa¹,

Ohtsuka²,

Yokoyama³

et al. 2002

FSTR

View full text Add to dashboard Cite

The microbial transglutaminase (TGase) from Streptomyces libani was purified from its culture broth and its enzymatic properties were compared with those of TGase from Streptoverticillium mobaraense var. TGase was purified by ion-exchange chromatography and size-exclusion chromatography. The specific activity of the main component was 10.7 unit/mg protein, lower than that of Streptoverticillium mobaraense var. (25 unit/mg). Several differences of enzymatic properties were found between the two enzymes. Optimum temperature, stability and gelation activity of TGase from Streptomyces libani were lower than those of TGase from Streptoverticillium mobaraense var, while, deamidation activity was higher. In addition, the existence of some TGases with different pI were suggested.

show abstract

Transglutaminase in sporulating cells of Bacillus subtilis.

Cited by 47 publications

References 25 publications

Assembly and Function of a Spore Coat-Associated Transglutaminase of Bacillus subtilis

Assembly and Function of a Spore Coat-Associated Transglutaminase of Bacillus subtilis

The Bacillus subtilis spore coat provides “eat resistance” during phagocytic predation by the protozoan Tetrahymena thermophila

Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

Contact Info

Product

Resources

About