Quaternary Structure of Fur Proteins, a New Subfamily of Tetrameric Proteins

The ferric uptake regulator (Fur) belongs to the family of the DNA-binding metal-responsive transcriptional regulators. Fur is a global regulator found in all proteobacteria. It controls the transcription of a wide variety of genes involved in iron metabolism but also in oxidative stress or virulenc...

Full description

Saved in:

Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 55; no. 10; pp. 1503 - 1515
Main Authors:	Pérard, Julien, Covès, Jacques, Castellan, Mathieu, Solard, Charles, Savard, Myriam, Miras, Roger, Galop, Sandra, Signor, Luca, Crouzy, Serge, Michaud-Soret, Isabelle, de Rosny, Eve
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 15-03-2016
Subjects:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacteriology Biochemistry, Molecular Biology DNA, Bacterial - chemistry DNA, Bacterial - genetics Escherichia coli - genetics Francisella tularensis - genetics Genomics Legionella pneumophila - genetics Life Sciences Microbiology and Parasitology Molecular Sequence Data Protein Structure, Quaternary - genetics Protein Structure, Secondary Pseudomonas aeruginosa - genetics Repressor Proteins - chemistry Repressor Proteins - genetics Yersinia - genetics
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	The ferric uptake regulator (Fur) belongs to the family of the DNA-binding metal-responsive transcriptional regulators. Fur is a global regulator found in all proteobacteria. It controls the transcription of a wide variety of genes involved in iron metabolism but also in oxidative stress or virulence factor synthesis. When bound to ferrous iron, Fur can bind to specific DNA sequences, called Fur boxes. This binding triggers the repression or the activation of gene expression, depending on the regulated genes. As a general view, Fur proteins are considered to be dimeric proteins both in solution and when bound to DNA. In this study, we have purified Fur from four pathogenic strains (Pseudomonas aeruginosa, Francisella tularensis, Yersinia pestis, and Legionella pneumophila) and compared them to Fur from Escherichia coli (EcFur), the best characterized of this family. By using a series of “in solution” techniques, including multiangle laser light scattering and small-angle X-ray scattering, as well as cross-linking experiments, we have shown that the Fur proteins can be classified into two groups, according to their quaternary structure. The group of dimers is represented by EcFur and YpFur and the group of very stable tetramers by PaFur, FtFur, and LpFur. Using PaFur as a case study, we also showed that the dissociation of the tetramers into dimers is necessary for binding of Fur to DNA, and that this dissociation requires the combined effect of metal ion binding and DNA proximity.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-2960 1520-4995
DOI:	10.1021/acs.biochem.5b01061