The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B fromEscherichia coli

Irritative voiding symptoms (e.g. increased frequency and urgency) occur in many common pathologic conditions such as urinary tract infections and bladder outlet obstruction, and these conditions are well-established to have underlying inflammation that directly triggers these symptoms. However, it remains unclear as to how such diverse stimuli individually generate a common inflammatory process. Jürg Tschopp provided substantial insight into this conundrum when, working with extracts from THP-1 cells, he reported the existence of the inflammasome. He described it as a structure that senses multiple diverse signals from intracellular/extracellular sources and pathogens and triggers inflammation by the maturation and release of the pro-inflammatory cytokines interleukin-1β and interleukin-18. Recently, many of these sensors were found in the bladder and the nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3, has been shown to be a central mediator of inflammation in several urological diseases. In this review, we introduce the nucleotide-binding domain, leucine-rich-containing family, pyrin domaincontaining-3 inflammasome, highlight its emerging role in several common urologic conditions, and speculate on the potential involvement of other inflammasomes in bladder pathology.

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Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron–sulfur cluster-binding domain

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444912045180 ◽

2013 ◽

Vol 69 (2) ◽

pp. 256-265 ◽

Cited By ~ 4

Author(s):

Xiaolu Li ◽

Wei Zhuo ◽

Jie Yu ◽

Jingpeng Ge ◽

Jinke Gu ◽

...

Keyword(s):

Abc Transporter ◽

Nucleotide Binding ◽

Binding Domain ◽

Nucleotide Binding Domain ◽

Iron Sulfur Cluster ◽

Sulfur Cluster ◽

Iron Sulfur

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Resistance to Bacitracin in Bacillus subtilis: Unexpected Requirement of the BceAB ABC Transporter in the Control of Expression of Its Own Structural Genes

Journal of Bacteriology ◽

10.1128/jb.01132-07 ◽

2007 ◽

Vol 189 (23) ◽

pp. 8636-8642 ◽

Cited By ~ 53

Author(s):

Remi Bernard ◽

Annick Guiseppi ◽

Marc Chippaux ◽

Maryline Foglino ◽

François Denizot

Keyword(s):

Signal Transduction ◽

Bacillus Subtilis ◽

Abc Transporter ◽

Defense Mechanism ◽

Response Regulator ◽

Nucleotide Binding ◽

Binding Domain ◽

Nucleotide Binding Domain ◽

Signal Transduction System ◽

Native Form

ABSTRACT The Bacillus subtilis BceAB ABC transporter involved in a defense mechanism against bacitracin is composed of a membrane-spanning domain and a nucleotide-binding domain. Induction of the structural bceAB genes requires the BceR response regulator and the BceS histidine kinase of a signal transduction system. However, despite the presence of such a transduction system and of bacitracin, no transcription from an unaltered bceA promoter is observed in cells lacking the BceAB transporter. Expression in trans of the BceAB transporter in these bceAB cells restores the transcription from the bceA promoter. Cells possessing a mutated nucleotide-binding domain of the transporter are also no longer able to trigger transcription from the bceA promoter in the presence of bacitracin, although the mutated ABC transporter is still bound to the membrane. In these cells, expression of the bceA promoter can no longer be detected, indicating that the ABC transporter not only must be present in the cell membrane, but also must be expressed in a native form for the induction of the bceAB genes. Several hypotheses are discussed to explain the simultaneous need for bacitracin, a native signal transduction system, and an active BceAB ABC transporter to trigger transcription from the bceA promoter.

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