Functional domains of colicin A
- 1 November 1988
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 2 (6), 807-811
- https://doi.org/10.1111/j.1365-2958.1988.tb00092.x
Abstract
A large number of mutations which introduce deletions in colicin A have been constructed. The partially deleted colicin A proteins were purifed and their activity in vivo (on sensitive cells) and in vitro (in planar lipid bilayers) was assayed. The receptor-binding properties of each protein were also analysed. From these results, we suggest that the NH2-terminal region of colicin A (residues 1 to 172) is involved in the translocation step through the outer membrane. The central region of colicin A (residues 173 to 336) contains the receptor-binding domain. The COOH-terminal domain (residues 389 to 592) carries the pore-forming activity.This publication has 32 references indexed in Scilit:
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