scholarly journals A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress

2008 ◽  
Vol 41 (5) ◽  
pp. 1159-1172 ◽  
Author(s):  
Hanne-Leena Hyyryläinen ◽  
Albert Bolhuis ◽  
Elise Darmon ◽  
Leila Muukkonen ◽  
Pertti Koski ◽  
...  
2002 ◽  
Vol 184 (20) ◽  
pp. 5661-5671 ◽  
Author(s):  
Elise Darmon ◽  
David Noone ◽  
Anne Masson ◽  
Sierd Bron ◽  
Oscar P. Kuipers ◽  
...  

ABSTRACT Bacteria need dedicated systems that allow appropriate adaptation to the perpetual changes in their environments. In Bacillus subtilis, two HtrA-like proteases, HtrA and HtrB, play critical roles in the cellular response to secretion and heat stresses. Transcription of these genes is induced by the high-level production of a secreted protein or by a temperature upshift. The CssR-CssS two-component regulatory system plays an essential role in this transcriptional activation. Transcription of the cssRS operon is autoregulated and can be induced by secretion stress, by the absence of either HtrA or HtrB, and by heat stress in a HtrA null mutant strain. Two start sites are used for cssRS transcription, only one of which is responsive to heat and secretion stress. The divergently transcribed htrB and cssRS genes share a regulatory region through which their secretion and heat stress-induced expression is linked. This study shows that CssRS-regulated genes represent a novel class of heat-inducible genes, which is referred to as class V and currently includes two genes: htrA and htrB.


FEBS Journal ◽  
2006 ◽  
Vol 273 (16) ◽  
pp. 3816-3827 ◽  
Author(s):  
Helga Westers ◽  
Lidia Westers ◽  
Elise Darmon ◽  
Jan Maarten van Dijl ◽  
Wim J. Quax ◽  
...  

2010 ◽  
Vol 33 (2) ◽  
pp. 333-340 ◽  
Author(s):  
Qinggang Guo ◽  
Shezeng Li ◽  
Xiuyun Lu ◽  
Baoqing Li ◽  
Ping Ma

2001 ◽  
Vol 183 (15) ◽  
pp. 4648-4651 ◽  
Author(s):  
Michihiro Hata ◽  
Mitsuo Ogura ◽  
Teruo Tanaka

ABSTRACT Expression of Bacillus subtilis aprE, encoding an extracellular alkaline protease, is positively regulated by phosphorylated DegU, the regulator of a two-component regulatory system, DegS-DegU. We found that the expression of anaprE′-′lacZ fusion was greatly reduced in a disruption mutant with a mutation of relA, which encodes the stringent factor RelA. The level of DegU in the relA mutant was similar to that in the wild-type cell. A relA degU double mutation did not result in a further decrease of theaprE′-′lacZ level found in a degU single mutant. The expression of the aprE′-′lacZ fusion in therelA mutant was stimulated by multicopy degR or the degU32(Hy) and degS200(Hy) mutations that cause the stabilization of phosphorylated DegU. Furthermore, the expression of sacB′-′lacZ, which is also dependent on phosphorylated DegU, was stimulated by the relA mutation, and this stimulation was not seen in the relA degU double mutant. These results show that RelA (or its product guanosine-3′,5′-bisdiphosphate [pp Gpp]) does not affect the phosphorylation of DegU and suggest that it participates in the expression of aprE and sacB through the regulation of DegU-dependent transcription.


2012 ◽  
Vol 194 (7) ◽  
pp. 1800-1814 ◽  
Author(s):  
D. Noone ◽  
E. Botella ◽  
C. Butler ◽  
A. Hansen ◽  
I. Jende ◽  
...  

2003 ◽  
Vol 49 (4) ◽  
pp. 1135-1144 ◽  
Author(s):  
Reiko Ohki ◽  
Giyanto ◽  
Kozue Tateno ◽  
Waka Masuyama ◽  
Shigeki Moriya ◽  
...  

Microbiology ◽  
2000 ◽  
Vol 146 (7) ◽  
pp. 1573-1583 ◽  
Author(s):  
Keisuke Fukuchi ◽  
Yasuhiro Kasahara ◽  
Kei Asai ◽  
Kazuo Kobayashi ◽  
Shigeki Moriya ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Genevieve S Dobihal ◽  
Yannick R Brunet ◽  
Josué Flores-Kim ◽  
David Z Rudner

Bacterial cells are encased in a peptidoglycan (PG) exoskeleton that protects them from osmotic lysis and specifies their distinct shapes. Cell wall hydrolases are required to enlarge this covalently closed macromolecule during growth, but how these autolytic enzymes are regulated remains poorly understood. Bacillus subtilis encodes two functionally redundant D,L-endopeptidases (CwlO and LytE) that cleave peptide crosslinks to allow expansion of the PG meshwork during growth. Here, we provide evidence that the essential and broadly conserved WalR-WalK two component regulatory system continuously monitors changes in the activity of these hydrolases by sensing the cleavage products generated by these enzymes and modulating their levels and activity in response. The WalR-WalK pathway is conserved among many Gram-positive pathogens where it controls transcription of distinct sets of PG hydrolases. Cell wall remodeling in these bacteria may be subject to homeostatic control mechanisms similar to the one reported here.


Microbiology ◽  
2005 ◽  
Vol 151 (9) ◽  
pp. 3041-3049 ◽  
Author(s):  
Kathrin Minnig ◽  
Vladimir Lazarevic ◽  
Blazenka Soldo ◽  
Catherine Mauël

The expression of the Bacillus subtilis W23 tar genes specifying the biosynthesis of the major wall teichoic acid, the poly(ribitol phosphate), was studied under phosphate limitation using lacZ reporter fusions. Three different regulation patterns can be deduced from these β-galactosidase activity data: (i) tarD and tarL gene expression is downregulated under phosphate starvation; (ii) tarA and, to a minor extent, tarB expression after an initial decrease unexpectedly increases; and (iii) tarO is not influenced by phosphate concentration. To dissect the tarA regulatory pattern, its two promoters were analysed under phosphate limitation: The P tarA -ext promoter is repressed under phosphate starvation by the PhoPR two-component system, whereas, under the same conditions, the P tarA -int promoter is upregulated by the action of an extracytoplasmic function (ECF) σ factor, σ M. In contrast to strain 168, σ M is activated in strain W23 in phosphate-depleted conditions, a phenomenon indirectly dependent on PhoPR, the two-component regulatory system responsible for the adaptation to phosphate starvation. These results provide further evidence for the role of σ M in cell-wall stress response, and suggest that impairment of cell-wall structure is the signal activating this ECF σ factor.


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