Molecular Characterization of the Essential Response Regulator Protein YycF in Bacillus subtilis

2003 ◽  
Vol 6 (3-4) ◽  
pp. 155-163 ◽  
Author(s):  
Takafumi Watanabe ◽  
Yoshiki Hashimoto ◽  
Yoshihito Umemoto ◽  
Daisuke Tatebe ◽  
Eiji Furuta ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Molecular Characterization ◽  
Response Regulator ◽  
Regulator Protein ◽  
Response Regulator Protein

Rational design and molecular characterization of a chimaeric response regulator protein

2001 ◽  
Vol 310 (2) ◽  
pp. 283-290 ◽  
Author(s):  
Andreas Bock ◽  
Marcus Bantscheff ◽  
Anne-Laure Perraud ◽  
Karsten Rippe ◽  
Verena Weiss ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Rational Design ◽  
Response Regulator ◽  
Regulator Protein ◽  
Response Regulator Protein

scholarly journals Unusual Heme Binding in the Bacterial Iron Response Regulator Protein: Spectral Characterization of Heme Binding to the Heme Regulatory Motif

Biochemistry ◽  
2011 ◽  
Vol 50 (6) ◽  
pp. 1016-1022 ◽  
Author(s):  
Haruto Ishikawa ◽  
Megumi Nakagaki ◽  
Ai Bamba ◽  
Takeshi Uchida ◽  
Hiroshi Hori ◽  
...  
Keyword(s):  
Response Regulator ◽  
Spectral Characterization ◽  
Heme Binding ◽  
Regulatory Motif ◽  
Regulator Protein ◽  
Iron Response Regulator ◽  
Response Regulator Protein

scholarly journals Candida albicans Response Regulator Gene SSK1 Regulates a Subset of Genes Whose Functions Are Associated with Cell Wall Biosynthesis and Adaptation to Oxidative Stress

2003 ◽  
Vol 2 (5) ◽  
pp. 1018-1024 ◽  
Author(s):  
Neeraj Chauhan ◽  
Diane Inglis ◽  
Elvira Roman ◽  
Jesus Pla ◽  
Dongmei Li ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Wall ◽  
Response Regulator ◽  
Cell Wall Biosynthesis ◽  
Regulator Protein ◽  
Two Component ◽  
Response Regulator Protein ◽  
Mutant Cells

ABSTRACT Ssk1p of Candida albicans is a putative response regulator protein of the Hog1 two-component signal transduction system. In Saccharomyces cerevisiae, the phosphorylation state of Ssk1p determines whether genes that promote the adaptation of cells to osmotic stress are activated. We have previously shown that C. albicans SSK1 does not complement the ssk1 mutant of S. cerevisiae and that the ssk1 mutant of C. albicans is not sensitive to sorbitol. In this study, we show that the C. albicans ssk1 mutant is sensitive to several oxidants, including hydrogen peroxide, t-butyl hydroperoxide, menadione, and potassium superoxide when each is incorporated in yeast extract-peptone-dextrose (YPD) agar medium. We used DNA microarrays to identify genes whose regulation is affected by the ssk1 mutation. RNA from mutant cells (strain CSSK21) grown in YPD medium for 3 h at 30°C was reverse transcribed and then compared with similarly prepared RNA from wild-type cells (CAF2). We observed seven genes from mutant cells that were consistently up regulated (three-fold or greater compared to CAF2). In S. cerevisiae, three (AHP1, HSP12, and PYC2) of the seven genes that were up regulated provide cells with an adaptation function in response to oxidative stress; another gene (GPH1) is regulated under stress conditions by Hog1p. Three other genes that are up regulated encode a cell surface protein (FLO1), a mannosyl transferase (MNN4-4), and a putative two-component histidine kinase (CHK1) that regulates cell wall biosynthesis in C. albicans. Of the down-regulated genes, ALS1 is a known cell adhesin in C. albicans. Verification of the microarray data was obtained by reverse transcription-PCR for HSP12, AHP1, CHK1, PYC2, GPH1, ALS1, MNN4-4, and FLO1. To further determine the function of Ssk1p in the Hog1p signal transduction pathway in C. albicans, we used Western blot analysis to measure phosphorylation of Hog1p in the ssk1 mutant of C. albicans when grown under either osmotic or oxidative stress. We observed that Hog1p was phosphorylated in the ssk1 mutant of C. albicans when grown in a hyperosmotic medium but was not phosphorylated in the ssk1 mutant when the latter was grown in the presence of hydrogen peroxide. These data indicate that C. albicans utilizes the Ssk1p response regulator protein to adapt cells to oxidative stress, while its role in the adaptation to osmotic stress is less certain. Further, SSK1 appears to have a regulatory function in some aspects of cell wall biosynthesis. Thus, the functions of C. albicans SSK1 differ from those of S. cerevisiae SSK1.

Isolation and Molecular Characterization of Thermostable Phytase from Bacillus subtilis (BSPhyARRMK33)

2015 ◽  
Vol 175 (6) ◽  
pp. 3058-3067 ◽  
Author(s):  
Chinreddy Subramanyam Reddy ◽  
V. Mohan Murali Achary ◽  
Mrinalini Manna ◽  
Jitender Singh ◽  
Tanushri Kaul ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Molecular Characterization

scholarly journals Switched or Not?: the Structure of Unphosphorylated CheY Bound to the N Terminus of FliM

2006 ◽  
Vol 188 (21) ◽  
pp. 7354-7363 ◽  
Author(s):  
Collin M. Dyer ◽  
Frederick W. Dahlquist
Keyword(s):  
Binding Site ◽  
Response Regulator ◽  
Phosphorylation Site ◽  
Active Role ◽  
Crystallographic Structure ◽  
Coupling Mechanism ◽  
Allosteric Communication ◽  
Regulator Protein ◽  
Target Binding ◽  
Response Regulator Protein

ABSTRACT Phosphorylation of Escherichia coli CheY increases its affinity for its target, FliM, 20-fold. The interaction between BeF3 −-CheY, a phosphorylated CheY (CheY∼P) analog, and the FliM sequence that it binds has been described previously in molecular detail. Although the conformation that unphosphorylated CheY adopts in complex with FliM was unknown, some evidence suggested that it is similar to that of CheY∼P. To resolve the issue, we have solved the crystallographic structure of unphosphorylated, magnesium(II)-bound CheY in complex with a synthetic peptide corresponding to the target region of FliM (the 16 N-terminal residues of FliM [FliM16]). While the peptide conformation and binding site are similar to those of the BeF3 −-CheY-FliM16 complex, the inactive CheY conformation is largely retained in the unphosphorylated Mg2+-CheY-FliM16 complex. Communication between the target binding site and the phosphorylation site, observed previously in biochemical experiments, is enabled by a network of conserved side chain interactions that partially mimic those observed in BeF3 −-activated CheY. This structure makes clear the active role that the β4-α4 loop plays in the Tyr87-Tyr106 coupling mechanism that enables allosteric communication between the phosphorylation site and the target binding surface. Additionally, this structure provides a high-resolution view of an intermediate conformation of a response regulator protein, which had been generally assumed to be two state.

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