Characterization of the DNA-binding site in the ferric uptake regulator protein from Escherichia coli by UV crosslinking and mass spectrometry

• Published in: FEBS letters Vol. 579; no. 25; pp. 5454 - 5460
• Main Authors: Tiss, Ali, Barre, Olivier, Michaud-Soret, Isabelle, Forest, Eric
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 24.10.2005; Wiley
• Subjects: Amino Acid Sequence; Bacterial Proteins; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacterial Proteins - radiation effects; Binding Sites; Biochemistry; Biochemistry, Molecular Biology; Consensus Sequence; DNA, Bacterial; DNA, Bacterial - chemistry; DNA, Bacterial - metabolism; DNA-binding; Escherichia coli; Escherichia coli - metabolism; Escherichia coli Proteins; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Ferric uptake regulator protein; Fur; Iron; Iron - metabolism; Life Sciences; Mass Spectrometry; Molecular Sequence Data; Peptide Mapping; Photocrosslinking; Protein Conformation; Pseudomonas aeruginosa; Pseudomonas aeruginosa - metabolism; Repressor Proteins; Repressor Proteins - chemistry; Repressor Proteins - metabolism; Repressor Proteins - radiation effects; Thymopoietins; Thymopoietins - chemistry; Thymopoietins - metabolism; Tyrosine; Tyrosine - chemistry; Tyrosine - metabolism; Ultraviolet Rays; Fur; Ferric uptake regulator protein; Photocrosslinking; Mass spectrometry; DNA-binding

Ferric uptake regulator protein (Fur) is activated by its cofactor iron to a state that binds to a specific DNA sequence called ‘Fur box’. Using mass spectrometry-based methods, we showed that Tyr 55 of Escherichia coli Fur, as well as the two thymines in positions 18 and 19 of the consensus Fur Box...