Crystal Structure of the C-terminal Domain of the Two-Component System Transmitter Protein Nitrogen Regulator II (NRII; NtrB), Regulator of Nitrogen Assimilation inEscherichia coli†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (21) ◽  
pp. 6670-6678 ◽  
Author(s):  
Yuanda Song ◽  
Daniel Peisach ◽  
Augen A. Pioszak ◽  
Zhaohui Xu ◽  
Alexander J. Ninfa
Keyword(s):  
Crystal Structure ◽  
Nitrogen Assimilation ◽  
Inescherichia Coli ◽  
Two Component System ◽  
Protein Nitrogen ◽  
Component System ◽  
Terminal Domain ◽  
Two Component

scholarly journals PhoB transcriptional activator binds hierarchically to pho box promoters

2012 ◽  
Vol 393 (10) ◽  
pp. 1165-1171 ◽  
Author(s):  
Alexandre G. Blanco ◽  
Albert Canals ◽  
Miquel Coll
Keyword(s):  
Crystal Structure ◽  
Molecular Mechanisms ◽  
Phosphate Uptake ◽  
Response Regulator ◽  
Sensor Kinase ◽  
Two Component System ◽  
Component System ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Two Component

Abstract The PhoR-PhoB phosphorelay is a bacterial two-component system that activates the transcription of several genes involved in phosphate uptake and assimilation. The response begins with the autophosphorylation of the sensor kinase PhoR, which activates the response regulator PhoB. Upon binding to the pho box DNA sequence, PhoB recruits the RNA polymerase and thereby activates the transcription of specific genes. To unveil hitherto unknown molecular mechanisms along the activation pathway, we report biochemical data characterizing the PhoB binding to promoters containing multiple pho boxes and describe the crystal structure of two PhoB DNA-binding domains bound in tandem to a 26-mer DNA.

scholarly journals PorA, a conserved C-terminal domain-containing protein, impacts the PorXY-SigP signaling of the type IX secretion system

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hideharu Yukitake ◽  
Mikio Shoji ◽  
Keiko Sato ◽  
Yusuke Handa ◽  
Mariko Naito ◽  
...  
Keyword(s):  
Cell Surface ◽  
Sigma Factor ◽  
Cysteine Proteases ◽  
Secretion System ◽  
Periodontal Pathogen ◽  
Two Component System ◽  
Component System ◽  
Terminal Domain ◽  
Two Component ◽  
Type Ix Secretion System

AbstractPorphyromonas gingivalis, a periodontal pathogen, translocates many virulence factors including the cysteine proteases referred to as gingipains to the cell surface via the type IX secretion system (T9SS). Expression of the T9SS component proteins is regulated by the tandem signaling of the PorXY two-component system and the ECF sigma factor SigP. However, the details of this regulatory pathway are still unknown. We found that one of the T9SS conserved C-terminal domain-containing proteins, PGN_0123, which we have designated PorA, is involved in regulating expression of genes encoding T9SS structural proteins and that PorA can be translocated onto the cell surface without the T9SS translocation machinery. X-ray crystallography revealed that PorA has a domain similar to the mannose-binding domain of Escherichia coli FimH, the tip protein of Type 1 pilus. Mutations in the cytoplasmic domain of the sensor kinase PorY conferred phenotypic recovery on the ΔporA mutant. The SigP sigma factor, which is activated by the PorXY two-component system, markedly decreased in the ΔporA mutant. These results strongly support a potential role for PorA in relaying a signal from the cell surface to the PorXY-SigP signaling pathway.

Control of Nitrogen Assimilation by the NRI-NRII Two-Component System of Enteric Bacteria

2014 ◽  
pp. 65-88 ◽  
Author(s):  
Alexander J. Ninfa ◽  
Mariette R. Atkinson ◽  
Emmanuel S. Kamberov ◽  
Junli Feng ◽  
Elizabeth G. Ninfa
Keyword(s):  
Nitrogen Assimilation ◽  
Enteric Bacteria ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction Proteins

2009 ◽  
Vol 192 (4) ◽  
pp. 1156-1159 ◽  
Author(s):  
Changsoo Chang ◽  
Christine Tesar ◽  
Minyi Gu ◽  
Gyorgy Babnigg ◽  
Andrzej Joachimiak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Signal Transduction ◽  
Histidine Kinase ◽  
Pas Domain ◽  
Two Component System ◽  
Component System ◽  
Sensor Histidine Kinase ◽  
Two Component ◽  
Sensor Kinases ◽  
Signal Transduction Proteins

ABSTRACT We present the crystal structure of the extracytoplasmic domain of the Bacillus subtilis PhoR sensor histidine kinase, part of a two-component system involved in adaptation to low environmental phosphate concentrations. In addition to the PhoR structure, we predict that the majority of the extracytoplasmic domains of B. subtilis sensor kinases will adopt a fold similar to the ubiquitous PAS domain.

scholarly journals Negative regulation of DNA repair gene (uvrA) expression by ArcA/ArcB two-component system inEscherichia coli

2005 ◽  
Vol 251 (2) ◽  
pp. 243-249 ◽  
Author(s):  
Hiroshi Ogasawara ◽  
Jun Teramoto ◽  
Satoshi Yamamoto ◽  
Kiyo Hirao ◽  
Kaneyoshi Yamamoto ◽  
...  
Keyword(s):  
Dna Repair ◽  
Negative Regulation ◽  
Inescherichia Coli ◽  
Two Component System ◽  
Repair Gene ◽  
Component System ◽  
Dna Repair Gene ◽  
Two Component
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