The cytotoxic domain of colicin E9 is a channel-forming endonuclease
نویسندگان
چکیده
منابع مشابه
Mechanism and cleavage specificity of the H-N-H endonuclease colicin E9.
Colicin endonucleases and the H-N-H family of homing enzymes share a common active site structural motif that has similarities to the active sites of a variety of other nucleases such as the non-specific endonuclease from Serratia and the sequence-specific His-Cys box homing enzyme I-PpoI. In contrast to these latter enzymes, however, it remains unclear how H-N-H enzymes cleave nucleic acid sub...
متن کاملCompetitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.
The natively disordered N-terminal 83-aa translocation (T) domain of E group nuclease colicins recruits OmpF to a colicin-receptor complex in the outer membrane (OM) as well as TolB in the periplasm of Escherichia coli, the latter triggering translocation of the toxin across the OM. We have identified the 16-residue TolB binding epitope in the natively disordered T-domain of the nuclease colici...
متن کاملConformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study.
Channel-forming colicins are bactericidal proteins that spontaneously insert into hydrophobic lipid bilayers. We have used magic-angle spinning solid-state nuclear magnetic resonance spectroscopy to examine the conformational differences between the water-soluble and the membrane-bound states of colicin Ia channel domain, and to study the effect of bound colicin on lipid bilayer structure and d...
متن کاملInteractions of TolB with the translocation domain of colicin E9 require an extended TolB box.
The mechanism by which enzymatic E colicins such as colicin E3 (ColE3) and ColE9 cross the outer membrane, periplasm, and cytoplasmic membrane to reach the cytoplasm and thus kill Escherichia coli cells is unique in prokaryotic biology but is poorly understood. This requires an interaction between TolB in the periplasm and three essential residues, D35, S37, and W39, of a pentapeptide sequence ...
متن کاملEnzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli.
The cytotoxicity of the bacterial toxin colicin E9 is due to a non-specific DNase that penetrates the cytoplasm of the infected organism and causes cell death. We report the first enzymological characterization of the overexpressed and purified 15 kDa DNase domain (E9 DNase) from this class of toxin. CD spectroscopy shows the E9 DNase to be structured in solution, and analytical ultracentrifuga...
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ژورنال
عنوان ژورنال: Nature Structural Biology
سال: 2002
ISSN: 1072-8368
DOI: 10.1038/nsb797