ArticleJournal of bacteriology1991
Membrane topography of ColE1 gene products: the immunity protein.
Article in Journal of bacteriology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 61 citations in OpenAlex.
- Channel domain of colicin A modifies the dimeric organization of its immunity protein.The Journal of biological chemistry · 2010Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Localization and functional analysis of PepI, the immunity peptide of Pep5-producing Staphylococcus epidermidis strain 5.Applied and environmental microbiology · 2004Article
- Translocation of colicin from the receptor to the inner cell membrane: function of the peptidoglycan layer.Folia microbiologica · 2002Article
- Colicin A immunity protein interacts with the hydrophobic helical hairpin of the colicin A channel domain in the Escherichia coli inner membrane.Journal of bacteriology · 2001Article
- Genetic organization of plasmid ColJs, encoding colicin Js activity, immunity, and release genes.Journal of bacteriology · 2001Article
- Identification of specific residues in colicin E1 involved in immunity protein recognition.Journal of bacteriology · 2001Article
- Membrane topology and insertion of membrane proteins: search for topogenic signals.Microbiology and molecular biology reviews : MMBR · 2000Review
- Molecular analysis of expression of the lantibiotic pep5 immunity phenotype.Applied and environmental microbiology · 1999Article
- Identification and properties of the genes encoding microcin E492 and its immunity protein.Journal of bacteriology · 1999Article
- The tip of the hydrophobic hairpin of colicin U is dispensable for colicin U activity but is important for interaction with the immunity protein.Journal of bacteriology · 1998Article
- Colicins--exocellular lethal proteins of Escherichia coli.Folia microbiologica · 1998Review
- Genetics of subtilin and nisin biosyntheses: biosynthesis of lantibiotics.Antonie van Leeuwenhoek · 1996Review
- Topology prediction of membrane proteins.Protein science : a publication of the Protein Society · 1996Article
- Immunity to lantibiotics.Antonie van Leeuwenhoek · 1996Review
- Evidence that the immunity protein inactivates colicin 5 immediately prior to the formation of the transmembrane channel.Journal of bacteriology · 1995Article
- Bacteriocins of gram-positive bacteria.Microbiological reviews · 1995Review
- Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3.Applied and environmental microbiology · 1995Article
- Colicins: structures, modes of action, transfer through membranes, and evolution.Archives of microbiology · 1994Review
- Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel.Protein science : a publication of the Protein Society · 1992Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The topography of the colicin E1 immunity (Imm) protein was determined from the positions of TnphoA and complementary lacZ fusions relative to the three long hydrophobic segments of the protein and site-directed substitution of charged for nonpolar residues in the proposed membrane-spanning segments. Inactivation of the Imm protein function required substitution and insertion of two such charges. It was concluded that the 113-residue colicin E1 Imm protein folds in the membrane as three trans-membrane alpha-helices, with the NH2 and COOH termini on the cytoplasmic and periplasmic sides of the membrane, respectively. The approximate spans of the three helices are Asn-9 to Ser-28, Ile-43 to Phe-62, and Leu-84 to Leu-104. An extrinsic highly charged segment, Lys-66 to Lys-74, containing seven charges in nine residues, extends into the cytoplasmic domain. The specificity of the colicin E1 Imm protein for interaction with the translocation apparatus and the colicin E1 ion channel is proposed to reside in its peripheral segments exposed on the surface of the inner membrane. These regions include the highly charged segment Lys-66 to Lys-83 (loop 2) and the short (approximately eight-residue) NH2 terminus on the cytoplasmic side, and Glu-29 to Val-44 (loop 1) and the COOH-terminal segment Gly-105 to Asn-113 on the periplasmic side.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.