Mutagenesis of conserved amino acids of Helicobacter pylori fur reveals residues important for function.

Journal of Bacteriology
Beth M CarpenterD Scott Merrell

Abstract

The ferric uptake regulator (Fur) of the medically important pathogen Helicobacter pylori is unique in that it has been shown to function as a repressor both in the presence of an Fe2+ cofactor and in its apo (non-Fe2+-bound) form. However, virtually nothing is known concerning the amino acid residues that are important for Fur functioning. Therefore, mutations in six conserved amino acid residues of H. pylori Fur were constructed and analyzed for their impact on both iron-bound and apo repression. In addition, accumulation of the mutant proteins, protein secondary structure, DNA binding ability, iron binding capacity, and the ability to form higher-order structures were also examined for each mutant protein. While none of the mutated residues completely abrogated the function of Fur, we were able to identify residues that were critical for both iron-bound and apo-Fur repression. One mutation, V64A, did not alter regulation of any target genes. However, each of the five remaining mutations showed an effect on either iron-bound or apo regulation. Of these, H96A, E110A, and E117A mutations altered iron-bound Fur regulation and were all shown to influence iron binding to different extents. Additionally, the H96A mutation was shown...Continue Reading

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Apr 29, 2009·PloS One·Beth M CarpenterD Scott Merrell

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Citations

Jun 24, 2010·The Journal of Microbiology·Shana MilesD Scott Merrell
Jan 9, 2014·PloS One·Patrick M ChongUNKNOWN Canadian Nosocomial Infection Surveillance Program (CNISP)
Oct 8, 2013·Journal of Bacteriology·Beth M CarpenterD Scott Merrell
Apr 23, 2011·Biophysical Chemistry·Hermes Reyes-CaballeroDavid P Giedroc
Jan 12, 2021·The Journal of Biological Chemistry·Tyree WilsonAngela Wilks

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