Bacillus stearothermophilusCell Shape Determinant Gene,mreCandmreD, and Their Stimulation of Protease Production inBacillus subtilis

Kubo, Michinori; Pierro, Dennis J.; Mochizuki, Yoshino; Kojima, Tatsuya; Yamazaki, Takenori; Satoh, Shuichi; Takizawa, Noboru; Kiyohara, Hohzoh

doi:10.1271/bbb.60.271

Cited by 9 publications

(9 citation statements)

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“…20 However, the deduced molecular mass of the isolated protease was 37 kDa, and the protein was found to be secreted, not membrane-bound. The work of Lee and Stewart noted that cells lacking MreC showed an accumulation of material at one side of the division septum, leading to a bending of the cellular shape.…”

Section: Implications Of Structure Alluding To An Enzymatic Role Of Mrecmentioning

confidence: 96%

High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC

Lovering

Strynadka

2007

Journal of Molecular Biology

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Section: Implications Of Structure Alluding To An Enzymatic Role Of Mrecmentioning

confidence: 96%

High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC

Lovering

Strynadka

2007

Journal of Molecular Biology

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“…Introduction of the mreC and mreD genes from Bacillus stearothermophilus into B. subtilis resulted in an overexpression of protease (18). This effect on protease expression required the presence of both mre determinants; no effect was seen with either determinant introduced alone into this host.…”

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confidence: 96%

Essential Nature of the mreC Determinant of Bacillus subtilis

Lee

Stewart

2003

J Bacteriol

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The mre genes of Escherichia coli and Bacillus subtilis are cell shape determination genes. Mutants affected in mre function are spheres instead of the normal rods. Although the mre determinants are not required for viability in E. coli, the mreB determinant is an essential gene in B. subtilis. Conflicting results have been reported as to whether the two membrane-associated proteins MreC and MreD are essential proteins. Furthermore, although the MreB protein has been studied in some detail, the roles of the MreC and MreD proteins in cell shape determination are unknown. We constructed a strain of B. subtilis in which expression of the mreC determinant is dependent upon the addition of isopropyl-␤-D-thiogalactopyranoside to the culture medium. Utilizing this conditional strain, it was shown that mreC is an essential gene in B. subtilis. Furthermore, it was shown that cells lacking sufficient quantities of MreC undergo morphological changes, namely, swelling and twisting of the cells, which is followed by cell lysis. Electron microscopy was utilized to demonstrate that a polymeric material accumulated at one side of the division septum of the cells and that the presence of this material correlated with the bending of the cell. The best explanation for the results is that the MreC protein is involved in the control of septal versus long-axis peptidoglycan synthesis, that cells lacking MreC perform aberrant septal peptidoglycan synthesis, and that lysis results from a deficiency in long-axis peptidoglycan synthesis.Bacteria have characteristic shapes, which are important taxonomic features. Most bacteria possess a fixed shape, although members of the genus Arthrobacter transition from rods to cocci depending on growth conditions (12). The bacterial cell wall is thought to be the major determinant of cell shape, as the purified murein sacculus retains the characteristic morphology of the cell, and specific changes in the chemical composition of the peptidoglycan have been noted in shape-altered mutants (25). However, shape determination is a complicated process, which involves not only the topology of peptidoglycan biosynthesis but also contributions of other components of the cell envelope as well as involvement of the cell division machinery. A mutation in the tagF (rodC) determinant of Bacillus subtilis gives rise to a shift from rod-shaped to spherical cells, indicating a contribution by teichoic acid to the determination of cell morphology (4,16,23).A model for bacterial shape regulation, the two-competingsites model, which relates cell shape to a balance between cell wall synthesis along the long axis of a rod-shaped cell and septum-specific peptidoglycan synthesis, has been proposed (21,24). This model proposes that shape determination in bacterial rods depends on the activity of two peptidoglycan synthesis reactions (sites) which are mutually exclusive. Consequently, the lateral wall is not extended during the septum formation step of cell division, and septal peptidoglycan synthesis does not occur during lat...

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“…Methods for the purification of the extracellular enzyme and manipulation of DNA were as described elsewhere ( Kubo & Imanaka 1988; Kubo et al . 1996 ).…”

Section: Methodsmentioning

confidence: 99%

Mechanism of thermostability in thermolysin – analysis of subsite S2 mutant enzymes of thermolysin

Kubo

Itoh

Nishikawa

et al. 1999

Letters in Applied Microbiology

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An aromatic amino acid at position 115 (tryptophan residue; subsite S2) in thermolysin is known to be essential for proteolytic activity of thermolysin. Mutant enzymes substituted by phenylalanine (W115F) and tyrosine (W115Y) at position 115 were expressed at similar levels as the wild type (WT) enzyme in Bacillus subtilis. The thermostability of the W115Y mutant enzyme was equal to that of the WT. However, that of the W115F mutant enzyme was significantly lower than the WT. Enzymatic kcat/Km values of W115F increased to about twice those of the WT, but W115F also seemed to promote increased autodegradation compared with the WT and W115Y enzymes.

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Bacillus stearothermophilusCell Shape Determinant Gene,mreCandmreD, and Their Stimulation of Protease Production inBacillus subtilis

Cited by 9 publications

References 0 publications

High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC

High-resolution Structure of the Major Periplasmic Domain from the Cell Shape-determining Filament MreC

Essential Nature of the mreC Determinant of Bacillus subtilis

Mechanism of thermostability in thermolysin – analysis of subsite S2 mutant enzymes of thermolysin

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