Abstract
Iron plays an integral role in a variety of physiological processes, and many pathogenic bacteria rely on iron‐dependent regulators (IDeRs) to sense cellular iron levels and regulate the transcription of iron storage and scavenging genes. The N‐terminal alpha‐helices of IDeRs are thought to play a significant role in dimerization and DNA‐binding. Accordingly, the length of the N‐termini in IDeR proteins varies little across a wide variety of species. Intriguingly, Actinomyces coleocanis possesses two IDeR open reading frames; one is the canonical length (“short”), while the second encodes an additional 39 amino acids at the N‐terminus (“long”). Here we present the expression, purification, and initial DNA‐binding studies of the short and long IDeR forms from the gram‐positive bacteria Actinomyces coleocanis.Support or Funding InformationThis work was supported by the Haines Biochemistry Fund and the John Beeson Student Research in Chemistry Fund.
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