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

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 w

SUBMITTER: Carpenter BM 

PROVIDER: S-EPMC2944535 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature