scholarly journals Thermal regulation of membrane lipid fluidity by a two-component system in Bacillus subtilis

2011 ◽  
Vol 39 (5) ◽  
pp. 362-366 ◽  
Author(s):  
L.M. Bredeston ◽  
D. Marciano ◽  
D. Albanesi ◽  
D. De Mendoza ◽  
J. M. Delfino
Keyword(s):  
Bacillus Subtilis ◽  
Membrane Lipid ◽  
Thermal Regulation ◽  
Two Component System ◽  
Component System ◽  
Lipid Fluidity ◽  
Two Component ◽  
Membrane Lipid Fluidity

The Bacillus subtilis ywkA gene encodes a malic enzyme and its transcription is activated by the YufL/YufM two-component system in response to malate

Microbiology ◽  
2003 ◽  
Vol 149 (9) ◽  
pp. 2331-2343 ◽  
Author(s):  
Thierry Doan ◽  
Pascale Servant ◽  
Shigeo Tojo ◽  
Hirotake Yamaguchi ◽  
Guillaume Lerondel ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Malic Enzyme ◽  
Northern Analysis ◽  
Two Component System ◽  
Extracellular Medium ◽  
Component System ◽  
Two Component ◽  
Transcriptome Comparison ◽  
Physiological Tests

A transcriptome comparison of a wild-type Bacillus subtilis strain growing under glycolytic or gluconeogenic conditions was performed. In particular, it revealed that the ywkA gene, one of the four paralogues putatively encoding a malic enzyme, was more transcribed during gluconeogenesis. Using a lacZ reporter fusion to the ywkA promoter, it was shown that ywkA was specifically induced by external malate and not subject to glucose catabolite repression. Northern analysis confirmed this expression pattern and demonstrated that ywkA is cotranscribed with the downstream ywkB gene. The ywkA gene product was purified and biochemical studies demonstrated its malic enzyme activity, which was 10-fold higher with NAD than with NADP (k cat/K m 102 and 10 s−1 mM−1, respectively). However, physiological tests with single and multiple mutant strains affected in ywkA and/or in ywkA paralogues showed that ywkA does not contribute to efficient utilization of malate for growth. Transposon mutagenesis allowed the identification of the uncharacterized YufL/YufM two-component system as being responsible for the control of ywkA expression. Genetic analysis and in vitro studies with purified YufM protein showed that YufM binds just upstream of ywkA promoter and activates ywkA transcription in response to the presence of malate in the extracellular medium, transmitted by YufL. ywkA and yufL/yufM could thus be renamed maeA for malic enzyme and malK/malR for malate kinase sensor/malate response regulator, respectively.

scholarly journals The PhoR/PhoP two-component system regulates fengycin production in Bacillus subtilis NCD-2 under low-phosphate conditions

2018 ◽  
Vol 17 (1) ◽  
pp. 149-157 ◽  
Author(s):  
Qing-gang GUO ◽  
Li-hong DONG ◽  
Pei-pei WANG ◽  
She-zeng LI ◽  
Wei-song ZHAO ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Catabolite repression of the citST two-component system in Bacillus subtilis

2006 ◽  
Vol 260 (2) ◽  
pp. 224-231 ◽  
Author(s):  
Guillermo D. Repizo ◽  
Víctor S. Blancato ◽  
Pablo D. Sender ◽  
Juke Lolkema ◽  
Christian Magni
Keyword(s):  
Bacillus Subtilis ◽  
Catabolite Repression ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Genomewide Transcriptional Analysis of the Cold Shock Response in Bacillus subtilis

2002 ◽  
Vol 184 (22) ◽  
pp. 6395-6402 ◽  
Author(s):  
Carsten L. Beckering ◽  
Leif Steil ◽  
Michael H. W. Weber ◽  
Uwe Völker ◽  
Mohamed A. Marahiel
Keyword(s):  
Bacillus Subtilis ◽  
Cold Shock ◽  
Research Field ◽  
Transcriptional Analysis ◽  
Two Component System ◽  
Two Dimensional Gel Electrophoresis ◽  
Component System ◽  
Cold Shock Response ◽  
Two Component ◽  
Shock Response

ABSTRACT Previous studies with two-dimensional gel electrophoresis techniques revealed that the cold shock response in Bacillus subtilis is characterized by rapid induction and accumulation of two classes of specific proteins, which have been termed cold-induced proteins (CIPs) and cold acclimatization proteins (CAPs), respectively. Only recently, the B. subtilis two-component system encoded by the desKR operon has been demonstrated to be essential for the cold-induced expression of the lipid-modifying desaturase Des, which is required for efficient cold adaptation of the membrane in the absence of isoleucine. At present, one of the most intriguing questions in this research field is whether DesKR plays a global role in cold signal perception and transduction in B. subtilis. In this report, we present the first genomewide transcriptional analysis of a cold-exposed bacterium and demonstrate that the B. subtilis two-component system DesKR exclusively controls the desaturase gene des and is not the cold-triggered regulatory system of global relevance. In addition to this, we identified a set of genes that might participate as novel players in the cold shock adaptation of B. subtilis. Two cold-induced genes, the elongation factor homolog ylaG and the σL-dependent transcriptional activator homolog yplP, have been examined by construction and analysis of deletion mutants.

Thermal regulation of membrane lipid fluidity in bacteria

1983 ◽  
Vol 8 (2) ◽  
pp. 49-52 ◽  
Author(s):  
Diego de Mendoza ◽  
John E. Cronan
Keyword(s):  
Membrane Lipid ◽  
Thermal Regulation ◽  
Lipid Fluidity ◽  
Membrane Lipid Fluidity

scholarly journals Immediate and Heterogeneous Response of the LiaFSR Two-Component System of Bacillus subtilis to the Peptide Antibiotic Bacitracin

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e53457 ◽  
Author(s):  
Sara Kesel ◽  
Andreas Mader ◽  
Carolin Höfler ◽  
Thorsten Mascher ◽  
Madeleine Leisner
Keyword(s):  
Bacillus Subtilis ◽  
Peptide Antibiotic ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis

PLoS Genetics ◽  
2015 ◽  
Vol 11 (6) ◽  
pp. e1005275 ◽  
Author(s):  
Elizabeth A. Libby ◽  
Lindsie A. Goss ◽  
Jonathan Dworkin
Keyword(s):  
Bacillus Subtilis ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Cell envelope gene expression in phosphate-limited Bacillus subtilis cells

Microbiology ◽  
2011 ◽  
Vol 157 (9) ◽  
pp. 2470-2484 ◽  
Author(s):  
Eric Botella ◽  
Sebastian Hübner ◽  
Karsten Hokamp ◽  
Annette Hansen ◽  
Paola Bisicchia ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Envelope ◽  
Expression Profiles ◽  
Phosphate Limitation ◽  
Envelope Gene ◽  
Two Component System ◽  
Cell Wall Metabolism ◽  
Component System ◽  
Two Component

The high phosphate content of Bacillus subtilis cell walls dictates that cell wall metabolism is an important feature of the PhoPR-mediated phosphate limitation response. Here we report the expression profiles of cell-envelope-associated and PhoPR regulon genes, determined by live cell array and transcriptome analysis, in exponentially growing and phosphate-limited B. subtilis cells. Control by the WalRK two-component system confers a unique expression profile and high level of promoter activity on the genes of its regulon with yocH and cwlO expression differing both qualitatively and quantitatively from all other autolysin-encoding genes examined. The activity of the PhoPR two-component system is restricted to the phosphate-limited state, being rapidly induced in response to the cognate stimulus, and can be sustained for an extended phosphate limitation period. Constituent promoters of the PhoPR regulon show heterogeneous induction profiles and very high promoter activities. Phosphate-limited cells also show elevated expression of the actin-like protein MreBH and reduced expression of the WapA cell wall protein and WprA cell wall protease indicating that cell wall metabolism in this state is distinct from that of exponentially growing and stationary-phase cells. The PhoPR response is very rapidly deactivated upon removal of the phosphate limitation stimulus with concomitant increased expression of cell wall metabolic genes. Moreover expression of genes encoding enzymes involved in sulphur metabolism is significantly altered in the phosphate-limited state with distinct perturbations being observed in wild-type 168 and AH024 (ΔphoPR) cells.

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