Identification and characterization of a UbK family kinase in Porphyromonas gingivalis which phosphorylates the RprY response regulator

Author(s):  
John D. Perpich ◽  
Lan Yakoumatos ◽  
Parker Johns ◽  
Kendall S. Stocke ◽  
Zackary R. Fitzsimonds ◽  
...  
1992 ◽  
Vol 42 (5) ◽  
pp. 689-695 ◽  
Author(s):  
Yukitaka MURAKAMI ◽  
Satoshi SHIZUKUISHI ◽  
Akira TSUNEMITSU ◽  
Kazuhisa NAKASHIMA ◽  
Yukio KATO ◽  
...  

2000 ◽  
Vol 54 (4) ◽  
pp. 373
Author(s):  
Akito Kusaba ◽  
Sumio Akifusa ◽  
Toshihiro Ansai ◽  
Tadamichi Takehara

Microbiology ◽  
2006 ◽  
Vol 152 (6) ◽  
pp. 1609-1620 ◽  
Author(s):  
Vinh D. Pham ◽  
Conrad W. Shebelut ◽  
Ivy R. Jose ◽  
David A. Hodgson ◽  
David E. Whitworth ◽  
...  

Phosphate regulation is complex in the developmental prokaryote Myxococcus xanthus, and requires at least four two-component systems (TCSs). Here, the identification and characterization of a member of one TCS, designated PhoP4, is reported. phoP4 insertion and in-frame deletion strains caused spore viability to be decreased by nearly two orders of magnitude, and reduced all three development-specific phosphatase activities by 80–90 % under phosphate-limiting conditions. Microarray and quantitative PCR analyses demonstrated that PhoP4 is also required for appropriate expression of the predicted pstSCAB–phoU operon of inorganic phosphate assimilation genes. Unlike the case for the other three M. xanthus Pho TCSs, the chromosomal region around phoP4 does not contain a partner histidine kinase gene. Yeast two-hybrid analyses reveal that PhoP4 interacts reciprocally with PhoR2, the histidine kinase of the Pho2 TCS; however, the existence of certain phenotypic differences between phoP4 and phoR2 mutants suggests that PhoP4 interacts with another, as-yet unidentified, histidine kinase.


2004 ◽  
Vol 51 (1) ◽  
pp. 253-262 ◽  
Author(s):  
Waltena Simpson ◽  
Teresa Olczak ◽  
Caroline A Genco

We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological significance of the HmuR-Kgp complex in heme utilization in P. gingivalis through the construction and characterization of a defined kgp mutant and a hmuR kgp double mutant in P. gingivalis A7436. The P. gingivalis kgp mutant exhibited a decreased ability to bind both hemin and hemoglobin. Growth of this strain with hemoglobin was delayed and its ability to utilize hemin as a sole iron source was diminished as compared to the wild type strain. Inactivation of both the hmuR and kgp genes resulted in further decreased ability of P. gingivalis to bind hemoglobin and hemin, as well as diminished ability to utilize either hemin or hemoglobin as a sole iron source. Collectively, these in vivo results further confirmed that both HmuR and Kgp are involved in the utilization of hemin and hemoglobin in P. gingivalis A7436.


2011 ◽  
Vol 10 (10) ◽  
pp. 1370-1374 ◽  
Author(s):  
Chirayu Desai ◽  
John Mavrianos ◽  
Neeraj Chauhan

ABSTRACT We report here the identification and characterization of a previously uncharacterized, two-component response regulator gene (orf19.5843) from Candida albicans . Because of its apparent functions in stress adaptation, we have named this gene SRR1 ( s tress r esponse r egulator 1). Disruption of SRR1 causes defects in hyphal development, reduced resistance to stress, and severe virulence attenuation in the mouse model of disseminated candidiasis.


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