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2 edition of Characterization of the TonB protein from Escherichia coli found in the catalog.

Characterization of the TonB protein from Escherichia coli

Jonathan Theodore Skare

Characterization of the TonB protein from Escherichia coli

insights into energy transduction between membranes

by Jonathan Theodore Skare

  • 307 Want to read
  • 36 Currently reading

Published .
Written in English

    Subjects:
  • Escherichia coli -- Metabolism.,
  • Biological transport, Active.,
  • Carrier proteins.,
  • Energy transfer.

  • Edition Notes

    Statementby Jonathan Theodore Skare.
    The Physical Object
    Paginationx, 145 leaves :
    Number of Pages145
    ID Numbers
    Open LibraryOL16910216M

    Using heterologous complementation of nanOU genes into an Escherichia coli strain devoid of outer membrane sialic acid permeases, we show that the nanOU system from the gut bacterium Bacteroides fragilis is functional and demonstrate its dependence on TonB for function. Yeast-two hybrid screening of E. coli proteins and integration with protein structure and genetic interaction data provides an extensive interactome resource. Efforts to map the Escherichia coli.

    Strategies for the Production of Recombinant Protein in Escherichia coli Gopal Jee Gopal • Awanish Kumar Springer Science+Business Media New York Abstract In the recent past years, a large number of proteins have been expressed in Escherichia coli with high productivity due to rapid development of genetic engi-neering wiztechinplanttraining.com by: A colicin is a type of bacteriocin produced by and toxic to some strains of Escherichia coli. Colicins are released into the environment to reduce competition from other bacterial wiztechinplanttraining.comns bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmic membrane, where they exert their cytotoxic effect, including depolarisation of the cytoplasmic membrane InterPro: IPR

    The Ton complex is a molecular motor that uses the proton gradient at the inner membrane of Gram-negative bacteria to generate force and movement, which are transmitted to transporters at the outer membrane, allowing the entry of nutrients into the periplasmic space. Despite decades of investigation and the recent flurry of structures being reported by X-ray crystallography and cryoEM, the Author: Herve Celia, Nicholas Noinaj, Susan K Buchanan. The urinary tract is among the most common sites of bacterial infection, and Escherichia coli is by far the most common species infecting this site. Individuals at high risk for symptomatic urinary tract infection (UTI) include neonates, preschool girls, sexually active women, and elderly women and men. E. coli that cause the majority of UTIs are thought to represent only a subset of the Cited by:


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Characterization of the TonB protein from Escherichia coli by Jonathan Theodore Skare Download PDF EPUB FB2

Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.).

In the absence of TonB these receptors bind their substrates but do not carry out active transport. Deletions within the 3′-end of the cloned Escherichia coli tonB gene were constructed and recombined into the chromosome.

Deletions affecting the last eight C-terminal amino acids (aa) yielded functionally active TonB, whereas deletion of the last 15 C-terminal aa, which removed the C-terminal hydrophobic region of TonB, abolished TonB function wiztechinplanttraining.com by: By its direct contact with outer membrane receptor BtuB, the cytoplasmic membrane transducer TonB delivers energy that mediates cyanocobalamin uptake in Escherichia coli.

This activity has been generally proposed to be the role of TonB in cyanocobalamin uptake. We now report the discovery and characterization of interactions between TonB and periplasmic binding protein wiztechinplanttraining.com by: Escherichia coli strains of serogroup O26 comprise two distinct groups of pathogens, characterized as enteropathogenic E.

coli (EPEC) and enterohemorrhagic E. coli (EHEC). Among the several genes related to type III secretion system-secreted effector proteins, espK was found to be highly specific for EHEC OH11 and its stx-negative derivative strains isolated in European wiztechinplanttraining.com by: 6.

The ExbD protein is involved in the energy-coupled transport of ferric siderophores, vitamin B12, and B-group colicins across the outer membrane of Escherichia coli. In order to study ExbD membrane topology, ExbD-beta-lactamase fusion proteins were constructed.

Cited by: Nov 17,  · For uptake of ferrichrome into bacterial cells, FhuA, a TonB-dependent outer membrane receptor of Escherichia coli, is required. The periplasmic protein FhuD binds and transfers ferrichrome to the cytoplasmic membrane-associated permease FhuB/C. We exploited phage display to map protein-protein interactions in the E.

coli cell envelope that Author: David M. Carter. characterization of escherichia coli strains and salmonella enterica serovars isolated in gallus gallus and their antimicrobial susceptibility by wesonga stephen makokha reg, no. i56//03 a thesis submitted to the school of pure and applied.

Characterization of the E. coli SOS response protein YbfE by Caitlin S. Kramer B.S. in Chemistry, Northeastern University A thesis submitted to The Faculty of the College of Science ofAuthor: Caitlin S. Kramer. Aug 08,  · Abstract. The sbcC and sbcD genes mediate palindrome inviability in Escherichia wiztechinplanttraining.comCD operon has been cloned into the plasmid pTrc99A under the control of the strong trc promoter and introduced into a strain carrying a chromosomal deletion of wiztechinplanttraining.com SbcC and SbcD polypeptides were overexpressed to 6% of total cell protein, and both polypeptides copurified in a four.

The Escherichia coli secB gene product is required for normal export of envelope proteins out of the cell cytoplasm. In this report, we present the identification and nucleotide sequence of the secB coding sequence. The secB structural gene overlaps almost completely with a predicted open reading frame (ORF) that is encoded on the opposite strand.

To establish the identity of the secB ORF, we Cited by: Nov 22,  · Abstract. The functional units within cells are often macromolecular complexes rather than single species. Production of these complexes as assembled homogenous samples is a prerequisite for their biophysical and structural characterization and hence Cited by: 8.

Escherichia coli (/ ˌ ɛ ʃ ə ˈ r ɪ k i ə ˈ k oʊ l aɪ /), also known as E. coli (/ ˌ iː ˈ k oʊ l aɪ /), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus Escherichia that is commonly found in the lower intestine of warm-blooded organisms (endotherms).Class: Gammaproteobacteria.

Postle K, Skare J () Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavag’e of its amino terminus. J Biol Chem – PubMed Google Scholar Pugsley AP () Nucleotide sequencing of the structural gene for colicin N reveals homology between the catalytic C-terminal domains of colicins A and Author: Hélène Benedetti, Lucienne Letellier, Roland Lloubes, Vincent Geli, Daniel Baty, Jean-Marie Pages, C.

The Escherichia coli outer membrane ferrichrome transporter FhuA was purified chromatographically in a neutral detergent (octyl glucoside or dodecyl maltoside). The amount of dodecyl maltoside bound to the protein ( ± g/g of FhuA) and the Stokes radius of the FhuA−dodecyl maltoside complex (RS = nm) were determined using size exclusion wiztechinplanttraining.com by: Energy-Dependent Conformational Change in the TolA Protein of Escherichia coli Involves Its N-Terminal Domain, TolQ, and TolR DNA sequence of the Escherichia coli tonB.

Molecular and genetic characterization of the TonB2-cluster TtpC protein in pathogenic vibrios Book. Full-text available. Escherichia coli TonB protein is required for the active transport. Burkholderia cenocepacia is an opportunistic pathogen prevalent in cystic fibrosis patients, which is particularly difficult to treat, causing chronic and eventually fatal infections.

The lack of effective treatment options makes evident the need to develop alternative therapeutic or prophylactic approaches. Vaccines, and live attenuated vaccines, are an unexplored avenue to treat B Cited by: 6.

Expression and Purification of Chimeric Protein. coli BL21(DE3) was transformed with expression plasmid pET-VEGI-CTT. Bacterial cultures were incubated at 37 ° C in LB growth medium with antibiotic selection ( ng/mL ampicillin), and grown until early log phase (A = –).

The targeted protein expression was induced at 37 ° C by the addition of IPTG to a final Cited by: 8. Abstract Biophysical Characterization of NleD: An effector protein from Escherichia coli OH7 Abhishek Chatterjee Pathogenic Escherichia coli strains (OH7) are one of the main causes behind the lethal E.

coli outbreaks in North America, UK and wiztechinplanttraining.com, a zinc-dependent endopeptidase. Escherichia coli (E. coli) is a very diverse bacterial species found naturally in the intestinal tract of humans and many other animal species.

Even though E. coli is known to be part of the normal gut microbiota, some strains – that are pathogenic – cause a wide variety of different intestinal and extraintestinal diseases (Marrs et al., ).Author: Marjanca Starčič Erjavec, Darja Žgur-Bertok.

A major outbreak caused by Escherichia coli of serotype OH4 spread throughout Europe in This large outbreak was caused by an unusual strain that is most similar to enteroaggregative E.

coli (EAEC) of serotype OH4. A significant difference, however, is the presence of a prophage encoding the Shiga toxin, which is characteristic of enterohemorrhagic E. coli (EHEC) wiztechinplanttraining.com by: The chromosome of Escherichia coli K‐12 contains a putative gene, yheB (chiA), at centisomewhose product shows sequence similarity with chitinases of bacterial and viral wiztechinplanttraining.com cloned the chiA (yheB) gene and demonstrated that it codes for a kDa periplasmic protein with endochitinase/lysozyme wiztechinplanttraining.com standard laboratory growth conditions, chiA expression is very .identified and classified largely in a series of biochemical tests or through molecular characterization.

Two bacterial species i.e., Pseudomonas aeroginosa, and E. coli were characterized by biochemical tests, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and FT-IR (Fourier Transform Infrared Spectroscopy).

Complex protein.