PMID:14672926
| Citation |
Cherny, I and Gazit, E (2004) The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J. Biol. Chem. 279:8252-61 |
|---|---|
| Abstract |
Although natively unfolded proteins are being observed increasingly, their physiological role is not well understood. Here, we demonstrate that the Escherichia coli YefM protein is a natively unfolded antitoxin, lacking secondary structure even at low temperature or in the presence of a stabilizing agent. This conformation of the protein is suggested to have a key role in its physiological regulatory activity. Because of the unfolded state of the protein, a linear determinant rather than a conformational one is presumably being recognized by its toxin partner, YoeB. A peptide array technology allowed the identification and validation of such a determinant. This recognition element may provide a novel antibacterial target. Indeed, a pair-constrained bioinformatic analysis facilitated the definite determination of novel YefM-YoeB toxin-antitoxin systems in a large number of bacteria including major pathogens such as Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis. Taken together, the YefM protein defines a new family of natively unfolded proteins. The existence of a large and conserved group of proteins with a clear physiologically relevant unfolded state serves as a paradigm to understand the structural basis of this state. |
| Links |
PubMed Online version:10.1074/jbc.M308263200 |
| Keywords |
Amino Acid Sequence; Binding Sites; Circular Dichroism; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Folding; Protein Structure, Secondary; Sequence Alignment; Surface Plasmon Resonance; Temperature |
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