The putative sensor histidine kinase VadJ coordinates development and sterigmatocystin production in Aspergillus nidulans

Author(s):  
Yanxia Zhao ◽  
Mi-Kyung Lee ◽  
Jieyin Lim ◽  
Heungyun Moon ◽  
Hee-Soo Park ◽  
...  
2008 ◽  
Vol 191 (3) ◽  
pp. 687-692 ◽  
Author(s):  
Francesca Scaramozzino ◽  
Andrea White ◽  
Marta Perego ◽  
James A. Hoch

ABSTRACT The Bacillus anthracis BA2291 gene codes for a sensor histidine kinase involved in the induction of sporulation. Genes for orthologs of the sensor domain of the BA2291 kinase exist in virulence plasmids in this organism, and these proteins, when expressed, inhibit sporulation by converting BA2291 to an apparent phosphatase of the sporulation phosphorelay. Evidence suggests that the sensor domains inhibit BA2291 by titrating its activating signal ligand. Studies with purified BA2291 revealed that this kinase is uniquely specific for GTP in the forward reaction and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP-specific histidine kinases, and modeling this motif in the structure of the kinase catalytic domain suggested how guanine binds to the region. A mutation in the putative coiled-coil linker between the sensor domain and the catalytic domains was found to decrease the rate of the forward autophosphorylation reaction and not affect the reverse reaction from phosphorylated Spo0F. The results suggest that the activating ligand for BA2291 is a critical signal for sporulation and in a limited concentration in the cell. Decreasing the response to it either by slowing the forward reaction through mutation or by titration of the ligand by expressing the plasmid-encoded sensor domains switches BA2291 from an inducer to an inhibitor of the phosphorelay and sporulation.


2001 ◽  
Vol 42 (2) ◽  
pp. 231-235 ◽  
Author(s):  
Chiharu Ueguchi ◽  
Hiromi Koizumi ◽  
Tomomi Suzuki ◽  
Takeshi Mizuno

2009 ◽  
Vol 16 (5) ◽  
pp. 1003-1009 ◽  
Author(s):  
Mobashar Hussain Urf Turabe Fazil ◽  
Sunil Kumar ◽  
Naidu Subbarao ◽  
Haushila Prasad Pandey ◽  
Durg Vijai Singh

2018 ◽  
Vol 293 (34) ◽  
pp. 13214-13223 ◽  
Author(s):  
Juan L. Teran-Melo ◽  
Gabriela R. Peña-Sandoval ◽  
Hortencia Silva-Jimenez ◽  
Claudia Rodriguez ◽  
Adrián F. Alvarez ◽  
...  

2008 ◽  
Vol 48 (supplement) ◽  
pp. S62
Author(s):  
Hironari Kamikubo ◽  
Tomonori Koyama ◽  
Michihiro Hayashi ◽  
Kumiko Shirai ◽  
Yoichi Yamazaki ◽  
...  

2008 ◽  
Vol 190 (21) ◽  
pp. 7147-7156 ◽  
Author(s):  
María Florencia Del Papa ◽  
Marta Perego

ABSTRACT Enterococcus faecalis is a gram-positive commensal bacterium of the human intestinal tract. Its opportunistic pathogenicity has been enhanced by the acquisition of multiple antibiotic resistances, making the treatment of enterococcal infections an increasingly difficult problem. The extraordinary capacity of this organism to colonize and survive in a wide variety of ecological niches is attributable, at least in part, to signal transduction pathways mediated by two-component systems (TCS). Here, the ability of E. faecalis to utilize ethanolamine as the sole carbon source is shown to be dependent upon the RR-HK17 (EF1633-EF1632) TCS. Ethanolamine is an abundant compound in the human intestine, and thus, the ability of bacteria to utilize it as a source of carbon and nitrogen may provide an advantage for survival and colonization. Growth of E. faecalis in a synthetic medium with ethanolamine was abolished in the response regulator RR17 mutant strain. Transcription of the response regulator gene was induced by the presence of ethanolamine. Ethanolamine induced a 15-fold increase in the rate of autophosphorylation in vitro of the HK17 sensor histidine kinase, indicating that this is the ligand recognized by the sensor domain of the kinase. These results assign a role to the RR-HK17 TCS as coordinator of the enterococcal response to specific nutritional conditions existing at the site of bacterial invasion, the intestinal tract of an animal host.


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