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  1. AU="Gordon, Jay E"
  2. AU="Huang, Mingsheng"
  3. AU="Karkowski, L"
  4. AU="Rana, Punam"
  5. AU=Kawasaki Shunsuke
  6. AU="Oliveira-Júnior, Gersiel"
  7. AU="Alvarado-Aguilar, Pablo"
  8. AU="Kyrin R. Hanning" AU="Kyrin R. Hanning"
  9. AU="Teixidor, Francesc"
  10. AU=Minhas Jasmit
  11. AU="Poe, Alyssa"
  12. AU="Ni, Bo"
  13. AU="Vemuri, Kiranmayi"
  14. AU="Hernández-Wolters, Benjamin"
  15. AU="Chobanova, Veronika"
  16. AU="Otten, Gisela"
  17. AU="Elhence, Anshuman"
  18. AU="Tinneberg, H-R"
  19. AU="Puro, Neeraj"
  20. AU=Yang Chi-Fu Jeffrey
  21. AU="Oliveira, Giuliana S"
  22. AU="Maria Cecilia Jocson"
  23. AU="Tollman, Stephen"
  24. AU="Cherry, Katie E."
  25. AU="Nazet, Ute"
  26. AU="Kranzer, K"
  27. AU="Avelino, Samuel"
  28. AU="Sun, Xiang-Dong"
  29. AU="Vogl, Thomas J."
  30. AU="Johnson, C R"
  31. AU="Gil-Pérez, Pablo"
  32. AU="Donno, Federica"
  33. AU="Vom Saal, Frederick S."
  34. AU="Gazzana, S"
  35. AU="Viswanadha, Vijaya P"
  36. AU="Anastasi, G A"
  37. AU="Romerosa, Antonio"
  38. AU=Gupta Gaorav P
  39. AU="Fernández-Susavila, Héctor"

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  1. Artikel ; Online: The Agrobacterium Ti Plasmids.

    Gordon, Jay E / Christie, Peter J

    Microbiology spectrum

    2014  Band 2, Heft 6

    Abstract: Agrobacterium tumefaciens is a plant pathogen with the capacity to deliver a segment of oncogenic DNA carried on a large plasmid called the tumor-inducing or Ti plasmid to susceptible plant cells. A. tumefaciens belongs to the class Alphaproteobacteria, ... ...

    Abstract Agrobacterium tumefaciens is a plant pathogen with the capacity to deliver a segment of oncogenic DNA carried on a large plasmid called the tumor-inducing or Ti plasmid to susceptible plant cells. A. tumefaciens belongs to the class Alphaproteobacteria, whose members include other plant pathogens (Agrobacterium rhizogenes), plant and insect symbionts (Rhizobium spp. and Wolbachia spp., respectively), human pathogens (Brucella spp., Bartonella spp., Rickettsia spp.), and nonpathogens (Caulobacter crescentus, Rhodobacter sphaeroides). Many species of Alphaproteobacteria carry large plasmids ranging in size from ∼100 kb to nearly 2 Mb. These large replicons typically code for functions essential for cell physiology, pathogenesis, or symbiosis. Most of these elements rely on a conserved gene cassette termed repABC for replication and partitioning, and maintenance at only one or a few copies per cell. The subject of this review is the ∼200-kb Ti plasmids carried by infectious strains of A. tumefaciens. We will summarize the features of this plasmid as a representative of the repABC family of megaplasmids. We will also describe novel features of this plasmid that enable A. tumefaciens cells to incite tumor formation in plants, sense and respond to an array of plant host and bacterial signal molecules, and maintain and disseminate the plasmid among populations of agrobacteria. At the end of this review, we will describe how this natural genetic engineer has been adapted to spawn an entire industry of plant biotechnology and review its potential for use in future therapeutic applications of plant and nonplant species.
    Mesh-Begriff(e) Agrobacterium tumefaciens/genetics ; DNA Replication ; DNA, Bacterial/genetics ; DNA, Bacterial/metabolism ; Plant Diseases/microbiology ; Plant Tumor-Inducing Plasmids ; Plants/microbiology
    Chemische Substanzen DNA, Bacterial
    Sprache Englisch
    Erscheinungsdatum 2014-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 2165-0497
    ISSN (online) 2165-0497
    DOI 10.1128/microbiolspec.PLAS-0010-2013
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.

    Gordon, Jay E / Costa, Tiago R D / Patel, Roosheel S / Gonzalez-Rivera, Christian / Sarkar, Mayukh K / Orlova, Elena V / Waksman, Gabriel / Christie, Peter J

    Molecular microbiology

    2017  Band 105, Heft 2, Seite(n) 273–293

    Abstract: Recent studies have shown that conjugation systems of Gram-negative bacteria are composed of distinct inner and outer membrane core complexes (IMCs and OMCCs, respectively). Here, we characterized the OMCC by focusing first on a cap domain that forms a ... ...

    Abstract Recent studies have shown that conjugation systems of Gram-negative bacteria are composed of distinct inner and outer membrane core complexes (IMCs and OMCCs, respectively). Here, we characterized the OMCC by focusing first on a cap domain that forms a channel across the outer membrane. Strikingly, the OMCC caps of the Escherichia coli pKM101 Tra and Agrobacterium tumefaciens VirB/VirD4 systems are completely dispensable for substrate transfer, but required for formation of conjugative pili. The pKM101 OMCC cap and extended pilus also are dispensable for activation of a Pseudomonas aeruginosa type VI secretion system (T6SS). Chimeric conjugation systems composed of the IMC
    Mesh-Begriff(e) Agrobacterium tumefaciens/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Bacterial Outer Membrane Proteins/physiology ; Bacterial Proteins/metabolism ; Conjugation, Genetic/genetics ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics ; Fimbriae, Bacterial/metabolism ; Protein Binding ; Protein Transport/genetics ; Type IV Secretion Systems/genetics ; Type IV Secretion Systems/metabolism ; Virulence Factors/metabolism
    Chemische Substanzen Bacterial Outer Membrane Proteins ; Bacterial Proteins ; DNA, Bacterial ; DNA-Binding Proteins ; Type IV Secretion Systems ; Virulence Factors
    Sprache Englisch
    Erscheinungsdatum 2017-05-18
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.13700
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Chimeric Coupling Proteins Mediate Transfer of Heterologous Type IV Effectors through the Escherichia coli pKM101-Encoded Conjugation Machine.

    Whitaker, Neal / Berry, Trista M / Rosenthal, Nathan / Gordon, Jay E / Gonzalez-Rivera, Christian / Sheehan, Kathy B / Truchan, Hilary K / VieBrock, Lauren / Newton, Irene L G / Carlyon, Jason A / Christie, Peter J

    Journal of bacteriology

    2016  Band 198, Heft 19, Seite(n) 2701–2718

    Abstract: Unlabelled: Bacterial type IV secretion systems (T4SSs) are composed of two major subfamilies, conjugation machines dedicated to DNA transfer and effector translocators for protein transfer. We show here that the Escherichia coli pKM101-encoded ... ...

    Abstract Unlabelled: Bacterial type IV secretion systems (T4SSs) are composed of two major subfamilies, conjugation machines dedicated to DNA transfer and effector translocators for protein transfer. We show here that the Escherichia coli pKM101-encoded conjugation system, coupled with chimeric substrate receptors, can be repurposed for transfer of heterologous effector proteins. The chimeric receptors were composed of the N-terminal transmembrane domain of pKM101-encoded TraJ fused to soluble domains of VirD4 homologs functioning in Agrobacterium tumefaciens, Anaplasma phagocytophilum, or Wolbachia pipientis A chimeric receptor assembled from A. tumefaciens VirD4 (VirD4At) mediated transfer of a MOBQ plasmid (pML122) and A. tumefaciens effector proteins (VirE2, VirE3, and VirF) through the pKM101 transfer channel. Equivalent chimeric receptors assembled from the rickettsial VirD4 homologs similarly supported the transfer of known or candidate effectors from rickettsial species. These findings establish a proof of principle for use of the dedicated pKM101 conjugation channel, coupled with chimeric substrate receptors, to screen for translocation competency of protein effectors from recalcitrant species. Many T4SS receptors carry sequence-variable C-terminal domains (CTDs) with unknown function. While VirD4At and the TraJ/VirD4At chimera with their CTDs deleted supported pML122 transfer at wild-type levels, ΔCTD variants supported transfer of protein substrates at strongly diminished or elevated levels. We were unable to detect binding of VirD4At's CTD to the VirE2 effector, although other VirD4At domains bound this substrate in vitro We propose that CTDs evolved to govern the dynamics of substrate presentation to the T4SS either through transient substrate contacts or by controlling substrate access to other receptor domains.
    Importance: Bacterial type IV secretion systems (T4SSs) display striking versatility in their capacity to translocate DNA and protein substrates to prokaryotic and eukaryotic target cells. A hexameric ATPase, the type IV coupling protein (T4CP), functions as a substrate receptor for nearly all T4SSs. Here, we report that chimeric T4CPs mediate transfer of effector proteins through the Escherichia coli pKM101-encoded conjugation system. Studies with these repurposed conjugation systems established a role for acidic C-terminal domains of T4CPs in regulating substrate translocation. Our findings advance a mechanistic understanding of T4CP receptor activity and, further, support a model in which T4SS channels function as passive conduits for any DNA or protein substrates that successfully engage with and pass through the T4CP specificity checkpoint.
    Mesh-Begriff(e) Conjugation, Genetic/physiology ; DNA, Bacterial ; Escherichia coli/genetics ; Escherichia coli/physiology ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Protein Domains ; Recombinant Fusion Proteins ; Type IV Secretion Systems/physiology
    Chemische Substanzen DNA, Bacterial ; Escherichia coli Proteins ; Recombinant Fusion Proteins ; Type IV Secretion Systems
    Sprache Englisch
    Erscheinungsdatum 2016-09-09
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00378-16
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Ud II Zs.50: Hefte anzeigen Standort:
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  4. Buch: Motion-picture production for industry

    Gordon, Jay E

    1961  

    Verfasserangabe Jay E. Gordon
    Sprache Englisch
    Umfang XVI, 352 S, Ill
    Verlag Macmillan Company u.a.
    Erscheinungsort New York, NY u.a.
    Dokumenttyp Buch
    Datenquelle Ehemaliges Sondersammelgebiet Küsten- und Hochseefischerei

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