Self-recognition by an intrinsically disordered protein.
The intrinsically disordered translocation domain (T-domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T-domain of colicin N known to bind to the helper protein TolA in target cells also interacts intramolecularly with folded regions of colicin N. We suggest that this specific self-recognition helps intrinsically disordered domains to bury their hydrophobic recognition motifs and protect them against degradation, showing that an impaired self-recognition leads to increased protease susceptibility.
School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich.
Oliver
O
Hecht
Helen
H
Ridley
Ruth
R
Boetzel
Allison
A
Lewin
Nick
N
Cull
David A
DA
Chalton
Jeremy H
JH
Lakey
Geoffrey R
GR
Moore
D000595:Amino Acid Sequence; D003087:Colicins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014443:Tyrosine / Q000737:chemistry
D003087:Colicins; D029968:Escherichia coli Proteins; C062093:tolA protein, E coli; D014443:Tyrosine