Functional domains of colicin A |
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| Authors: | D Baty M Frenette R Lioubès V Geli S P Howard F Pattus C Lazdunski |
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| Institution: | Centre de Biochimie et de Biologie Moléculaire du C.N.R.S., 31 Chemin Joseph Aiguier, BP71, 13402 Marseille Cedex 9, France.;European Molecular Biology Laboratory, Postfach 10.2209, Meyerhofstrasse 1, 6900 Heidelberg, FRG. |
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| Abstract: | A large number of mutations which introduce deletions in colicin A have been constructed. The partially deleted colicin A proteins were purified 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. |
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