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  1. Article: Xenogeneic Regulation of the Bacterial Transcription Machinery

    Tabib-Salazar, Aline / Matthews, Steve J / Mulvenna, Nancy / Severinov, Konstantin / Wigneshweraraj, Sivaramesh

    Journal of molecular biology. 2019 Sept. 20, v. 431, no. 20

    2019  

    Abstract: The parasitic life cycle of viruses involves the obligatory subversion of the host's macromolecular processes for efficient viral progeny production. Viruses that infect bacteria, bacteriophages (phages), are no exception and have evolved sophisticated ... ...

    Abstract The parasitic life cycle of viruses involves the obligatory subversion of the host's macromolecular processes for efficient viral progeny production. Viruses that infect bacteria, bacteriophages (phages), are no exception and have evolved sophisticated ways to control essential biosynthetic machineries of their bacterial prey to benefit phage development. The xenogeneic regulation of bacterial cell function is a poorly understood area of bacteriology. The activity of the bacterial transcription machinery, the RNA polymerase (RNAP), is often regulated by a variety of mechanisms involving small phage-encoded proteins. In this review, we provide a brief overview of known phage proteins that interact with the bacterial RNAP and compare how two prototypical phages of Escherichia coli, T4 and T7, use small proteins to “puppeteer” the bacterial RNAP to ensure a successful infection.
    Keywords bacteria ; bacteriology ; bacteriophages ; biosynthesis ; DNA-directed RNA polymerase ; Escherichia coli ; progeny ; proteins ; transcription (genetics)
    Language English
    Dates of publication 2019-0920
    Size p. 4078-4092.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.02.008
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  2. Article ; Online: Xenogeneic modulation of the ClpCP protease of

    Mulvenna, Nancy / Hantke, Ingo / Burchell, Lynn / Nicod, Sophie / Bell, David / Turgay, Kürşad / Wigneshweraraj, Sivaramesh

    The Journal of biological chemistry

    2019  Volume 294, Issue 46, Page(s) 17501–17511

    Abstract: Like eukaryotic and archaeal viruses, which coopt the host's cellular pathways for their replication, bacteriophages have evolved strategies to alter the metabolism of their bacterial host. SPO1 bacteriophage infection ... ...

    Abstract Like eukaryotic and archaeal viruses, which coopt the host's cellular pathways for their replication, bacteriophages have evolved strategies to alter the metabolism of their bacterial host. SPO1 bacteriophage infection of
    MeSH term(s) Bacillus Phages/chemistry ; Bacillus Phages/genetics ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacillus subtilis/virology ; Cell Division/genetics ; DNA Replication/genetics ; DNA, Viral/chemistry ; DNA, Viral/genetics ; Endopeptidases/chemistry ; Endopeptidases/genetics ; Viral Proteins/chemistry ; Viral Proteins/genetics
    Chemical Substances DNA, Viral ; Viral Proteins ; Endopeptidases (EC 3.4.-)
    Language English
    Publishing date 2019-07-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA119.010007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Xenogeneic Regulation of the Bacterial Transcription Machinery.

    Tabib-Salazar, Aline / Mulvenna, Nancy / Severinov, Konstantin / Matthews, Steve J / Wigneshweraraj, Sivaramesh

    Journal of molecular biology

    2019  Volume 431, Issue 20, Page(s) 4078–4092

    Abstract: The parasitic life cycle of viruses involves the obligatory subversion of the host's macromolecular processes for efficient viral progeny production. Viruses that infect bacteria, bacteriophages (phages), are no exception and have evolved sophisticated ... ...

    Abstract The parasitic life cycle of viruses involves the obligatory subversion of the host's macromolecular processes for efficient viral progeny production. Viruses that infect bacteria, bacteriophages (phages), are no exception and have evolved sophisticated ways to control essential biosynthetic machineries of their bacterial prey to benefit phage development. The xenogeneic regulation of bacterial cell function is a poorly understood area of bacteriology. The activity of the bacterial transcription machinery, the RNA polymerase (RNAP), is often regulated by a variety of mechanisms involving small phage-encoded proteins. In this review, we provide a brief overview of known phage proteins that interact with the bacterial RNAP and compare how two prototypical phages of Escherichia coli, T4 and T7, use small proteins to "puppeteer" the bacterial RNAP to ensure a successful infection.
    MeSH term(s) Bacterial Proteins/metabolism ; Bacteriophage T4/genetics ; Bacteriophage T4/growth & development ; Bacteriophage T7/genetics ; Bacteriophage T7/growth & development ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/genetics ; Escherichia coli/virology ; Gene Expression Regulation, Bacterial ; Microbial Interactions ; Transcription, Genetic ; Viral Proteins/metabolism
    Chemical Substances Bacterial Proteins ; Viral Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6)
    Language English
    Publishing date 2019-02-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.02.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Bacteriophage protein PEIP is a potent Bacillus subtilis enolase inhibitor.

    Zhang, Kaining / Li, Shanshan / Wang, Yawen / Wang, Zhihao / Mulvenna, Nancy / Yang, Hang / Zhang, Peipei / Chen, Huan / Li, Yan / Wang, Hongliang / Gao, Yongxiang / Wigneshweraraj, Sivaramesh / Matthews, Steve / Zhang, Kaiming / Liu, Bing

    Cell reports

    2022  Volume 40, Issue 1, Page(s) 111026

    Abstract: Enolase is a highly conserved enzyme that presents in all organisms capable of glycolysis or fermentation. Its immediate product phosphoenolpyruvate is essential for other important processes like peptidoglycan synthesis and the phosphotransferase system ...

    Abstract Enolase is a highly conserved enzyme that presents in all organisms capable of glycolysis or fermentation. Its immediate product phosphoenolpyruvate is essential for other important processes like peptidoglycan synthesis and the phosphotransferase system in bacteria. Therefore, enolase inhibitors are of great interest. Here, we report that Gp60, a phage-encoded enolase inhibitor protein (PEIP) of bacteriophage SPO1 for Bacillus subtilis, is an enolase inhibitor. PEIP-expressing bacteria exhibit growth attenuation, thinner cell walls, and safranin color in Gram staining owing to impaired peptidoglycan synthesis. We solve the structure of PEIP-enolase tetramer and show that PEIP disassembles enolase by disrupting the basic dimer unit. The structure reveals that PEIP does not compete for substrate binding but induces a cascade of conformational changes that limit accessibility to the enolase catalytic site. This phage-inspired disassembly of enolase represents an alternative strategy for the development of anti-microbial drugs.
    MeSH term(s) Bacillus subtilis/metabolism ; Bacteriophages/metabolism ; Catalytic Domain ; Peptidoglycan/metabolism ; Phosphopyruvate Hydratase/metabolism
    Chemical Substances Peptidoglycan ; Phosphopyruvate Hydratase (EC 4.2.1.11)
    Language English
    Publishing date 2022-07-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2022.111026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: A Bacteriophage DNA Mimic Protein Employs a Non-specific Strategy to Inhibit the Bacterial RNA Polymerase.

    Wang, Zhihao / Wang, Hongliang / Mulvenna, Nancy / Sanz-Hernandez, Maximo / Zhang, Peipei / Li, Yanqing / Ma, Jia / Wang, Yawen / Matthews, Steve / Wigneshweraraj, Sivaramesh / Liu, Bing

    Frontiers in microbiology

    2021  Volume 12, Page(s) 692512

    Abstract: DNA mimicry by proteins is a strategy that employed by some proteins to occupy the binding sites of the DNA-binding proteins and deny further access to these sites by DNA. Such proteins have been found in bacteriophage, eukaryotic virus, prokaryotic, and ...

    Abstract DNA mimicry by proteins is a strategy that employed by some proteins to occupy the binding sites of the DNA-binding proteins and deny further access to these sites by DNA. Such proteins have been found in bacteriophage, eukaryotic virus, prokaryotic, and eukaryotic cells to imitate non-coding functions of DNA. Here, we report another phage protein Gp44 from bacteriophage SPO1 of
    Language English
    Publishing date 2021-06-02
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2021.692512
    Database MEDical Literature Analysis and Retrieval System OnLINE

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