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.
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Selected References
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- Achtman M., Manning P. A., Edelbluth C., Herrlich P. Export without proteolytic processing of inner and outer membrane proteins encoded by F sex factor tra cistrons in Escherichia coli minicells. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4837–4841. doi: 10.1073/pnas.76.10.4837. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Argos P., Rao J. K., Hargrave P. A. Structural prediction of membrane-bound proteins. Eur J Biochem. 1982 Nov 15;128(2-3):565–575. doi: 10.1111/j.1432-1033.1982.tb07002.x. [DOI] [PubMed] [Google Scholar]
- Bazaral M., Helinski D. R. Circular DNA forms of colicinogenic factors E1, E2 and E3 from Escherichia coli. J Mol Biol. 1968 Sep 14;36(2):185–194. doi: 10.1016/0022-2836(68)90374-4. [DOI] [PubMed] [Google Scholar]
- Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bolívar F. Molecular cloning vectors derived from the CoLE1 type plasmid pMB1. Life Sci. 1979 Sep 3;25(10):807–817. doi: 10.1016/0024-3205(79)90538-1. [DOI] [PubMed] [Google Scholar]
- Brosius J., Holy A. Regulation of ribosomal RNA promoters with a synthetic lac operator. Proc Natl Acad Sci U S A. 1984 Nov;81(22):6929–6933. doi: 10.1073/pnas.81.22.6929. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brunden K. R., Cramer W. A., Cohen F. S. Purification of a small receptor-binding peptide from the central region of the colicin E1 molecule. J Biol Chem. 1984 Jan 10;259(1):190–196. [PubMed] [Google Scholar]
- Bullock J. O., Cohen F. S., Dankert J. R., Cramer W. A. Comparison of the macroscopic and single channel conductance properties of colicin E1 and its COOH-terminal tryptic peptide. J Biol Chem. 1983 Aug 25;258(16):9908–9912. [PubMed] [Google Scholar]
- Cleveland M. V., Slatin S., Finkelstein A., Levinthal C. Structure-function relationships for a voltage-dependent ion channel: properties of COOH-terminal fragments of colicin E1. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3706–3710. doi: 10.1073/pnas.80.12.3706. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cramer W. A., Dankert J. R., Uratani Y. The membrane channel-forming bacteriocidal protein, colicin El. Biochim Biophys Acta. 1983 Mar 21;737(1):173–193. doi: 10.1016/0304-4157(83)90016-3. [DOI] [PubMed] [Google Scholar]
- Dankert J. R., Uratani Y., Grabau C., Cramer W. A., Hermodson M. On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization. J Biol Chem. 1982 Apr 10;257(7):3857–3863. [PubMed] [Google Scholar]
- DePamphilis M. L., Adler J. Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer, lipopolysaccharide membrane and the cyoplasmic membrane. J Bacteriol. 1971 Jan;105(1):396–407. doi: 10.1128/jb.105.1.396-407.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Di Masi D. R., White J. C., Schnaitman C. A., Bradbeer C. Transport of vitamin B12 in Escherichia coli: common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope. J Bacteriol. 1973 Aug;115(2):506–513. doi: 10.1128/jb.115.2.506-513.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Filip C., Fletcher G., Wulff J. L., Earhart C. F. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol. 1973 Sep;115(3):717–722. doi: 10.1128/jb.115.3.717-722.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirose A., Kumagai J., Imahori K. Dessociation and reconstitution of colicin E3 and immunity substance complex. J Biochem. 1976 Feb;79(2):305–311. doi: 10.1093/oxfordjournals.jbchem.a131073. [DOI] [PubMed] [Google Scholar]
- Inselburg J., Applebaum B. Proteins synthesized in minicells containing plasmid ColE1 and its mutants. J Bacteriol. 1978 Mar;133(3):1444–1451. doi: 10.1128/jb.133.3.1444-1451.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Konisky J., Cowell B. S. Interaction of colicin Ia with bacterial cells. Direct measurement of Ia-receptor interaction. J Biol Chem. 1972 Oct 25;247(20):6524–6529. [PubMed] [Google Scholar]
- Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
- Levisohn R., Konisky J., Nomura M. Interaction of colicins with bacterial cells. IV. Immunity breakdown studied with colicins Ia and Ib. J Bacteriol. 1968 Sep;96(3):811–821. doi: 10.1128/jb.96.3.811-821.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maeda A., Nomura M. Interaction of colicins with bacterial cells. I. Studies with radioactive colicins. J Bacteriol. 1966 Feb;91(2):685–694. doi: 10.1128/jb.91.2.685-694.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mandel M., Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970 Oct 14;53(1):159–162. doi: 10.1016/0022-2836(70)90051-3. [DOI] [PubMed] [Google Scholar]
- Mankovich J. A., Lai P. H., Gokul N., Konisky J. Organization of the colicin Ib gene. Promoter structure and immunity domain. J Biol Chem. 1984 Jul 25;259(14):8764–8768. [PubMed] [Google Scholar]
- Melchior W. B., Jr, Fahrney D. Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with alpha-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4. Biochemistry. 1970 Jan 20;9(2):251–258. doi: 10.1021/bi00804a010. [DOI] [PubMed] [Google Scholar]
- Miles E. W. Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 1977;47:431–442. doi: 10.1016/0076-6879(77)47043-5. [DOI] [PubMed] [Google Scholar]
- Morita M., Oka A. The structure of a transcriptional unit on colicin E1 plasmid. Eur J Biochem. 1979 Jul;97(2):435–443. doi: 10.1111/j.1432-1033.1979.tb13131.x. [DOI] [PubMed] [Google Scholar]
- Nossal N. G., Heppel L. A. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J Biol Chem. 1966 Jul 10;241(13):3055–3062. [PubMed] [Google Scholar]
- Ohno-Iwashita Y., Imahori K. Assignment of the functional loci in the colicin E1 molecule by characterization of its proteolytic fragments. J Biol Chem. 1982 Jun 10;257(11):6446–6451. [PubMed] [Google Scholar]
- Oka A., Nomura N., Morita M., Sugisaki H., Sugimoto K., Takanami M. Nucleotide sequence of small ColE1 derivatives: structure of the regions essential for autonomous replication and colicin E1 immunity. Mol Gen Genet. 1979 May 4;172(2):151–159. doi: 10.1007/BF00268276. [DOI] [PubMed] [Google Scholar]
- Patient R. K. Characterization of in vitro transcription initiation and termination sites in Col E1 DNA. Nucleic Acids Res. 1979 Jun 25;6(8):2647–2665. doi: 10.1093/nar/6.8.2647. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sancar A., Hack A. M., Rupp W. D. Simple method for identification of plasmid-coded proteins. J Bacteriol. 1979 Jan;137(1):692–693. doi: 10.1128/jb.137.1.692-693.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schnaitman C. A. Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli. J Bacteriol. 1970 Nov;104(2):890–901. doi: 10.1128/jb.104.2.890-901.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sidikaro J., Nomura M. E3 immunity substance. A protein from e3-colicinogenic cells that accounts for their immunity to colicin E3. J Biol Chem. 1974 Jan 25;249(2):445–453. [PubMed] [Google Scholar]
- Stüber D., Bujard H. Organization of transcriptional signals in plasmids pBR322 and pACYC184. Proc Natl Acad Sci U S A. 1981 Jan;78(1):167–171. doi: 10.1073/pnas.78.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suit J. L., Fan M. L., Sabik J. F., Labarre R., Luria S. E. Alternative forms of lethality in mitomycin C-induced bacteria carrying ColE1 plasmids. Proc Natl Acad Sci U S A. 1983 Jan;80(2):579–583. doi: 10.1073/pnas.80.2.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tilby M., Hindennach I., Henning U. Bypass of receptor-mediated resistance to colicin E3 in Escherichia coli K-12. J Bacteriol. 1978 Dec;136(3):1189–1191. doi: 10.1128/jb.136.3.1189-1191.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weaver C. A., Redborg A. H., Konisky J. Plasmid-determined immunity of Escherichia coli K-12 to colicin Ia Is mediated by a plasmid-encoded membrane protein. J Bacteriol. 1981 Dec;148(3):817–828. doi: 10.1128/jb.148.3.817-828.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Widger W. R., Cramer W. A., Herrmann R. G., Trebst A. Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane. Proc Natl Acad Sci U S A. 1984 Feb;81(3):674–678. doi: 10.1073/pnas.81.3.674. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van den Elzen P. J., Gaastra W., Spelt C. E., de Graaf F. K., Veltkamp E., Nijkamp H. J. Molecular structure of the immunity gene and immunity protein of the bacteriocinogenic plasmid Clo DF13. Nucleic Acids Res. 1980 Oct 10;8(19):4349–4363. doi: 10.1093/nar/8.19.4349. [DOI] [PMC free article] [PubMed] [Google Scholar]
- von Heijne G., Blomberg C. Trans-membrane translocation of proteins. The direct transfer model. Eur J Biochem. 1979 Jun;97(1):175–181. doi: 10.1111/j.1432-1033.1979.tb13100.x. [DOI] [PubMed] [Google Scholar]