Previous Article | Next Article ![]()
Journal of Bacteriology, March 2001, p. 2132-2136, Vol. 183, No. 6
Department of Biological Sciences, Purdue
University, West Lafayette, Indiana 47906-1392
Received 11 October 2000/Accepted 26 December 2000
The basis of specificity between pore-forming colicins and immunity
proteins was explored by interchanging residues between colicins E1
(ColE1) and 10 (Col10) and testing for altered recognition by their
respective immunity proteins, Imm and Cti. A total of 34 divergent
residues in the pore-forming domain of ColE1 between residues 419 and
501, a region previously shown to contain the specificity determinants
for Imm, were mutagenized to the corresponding Col10 sequences.
The residue changes most effective in converting ColE1 to the Col10
phenotype are residue 448 at the N terminus of helix VI and residues
470, 472, and 474 at the C terminus of helix VII. Mutagenesis of helix
VI residues 416 to 419 in Col10 to the corresponding ColE1 sequence
resulted in increased recognition by Imm and loss of recognition by Cti.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.6.2132-2136.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification of Specific Residues in Colicin E1
Involved in Immunity Protein Recognition
*
Corresponding author. Mailing address: Department of
Biological Sciences, Purdue University, West Lafayette, IN 47906-1392. Phone: (765) 494-4927. Fax: (765) 496-1189. E-mail:
mlindebe{at}bilbo.bio.purdue.edu.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»