Localization of the immunity protein-reactive domain in unmodified and chemically modified COOH-terminal peptides of colicin E1.

Abstract:

:The region of the colicin E1 polypeptide that interacts with immunity protein has been localized to a 168-residue COOH-terminal peptide. This is the length of a proteolytically generated peptide fragment of colicin E1 against which imm+ function can be demonstrated in osmotically shocked cells. The role of particular amino acids of the COOH-terminal peptide in the expression of the immune phenotype was studied. Chemical modification showed that the two histidine residues (His 427 and His 440) and the single cysteine residue (Cys 505) present in the COOH-terminal peptide were not necessary for the colicin-immunity protein interaction. The immunity protein was localized in the cytoplasmic membrane fraction, consistent with previous work of others on the colicin Ia immunity protein and the prediction from the immunity protein amino acid sequence that it is a hydrophobic protein. The distribution of hydrophobic residues along the immunity polypeptide was calculated.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Bishop LJ,Bjes ES,Davidson VL,Cramer WA

doi

10.1128/JB.164.1.237-244.1985

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

237-44

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

164

pub_type

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