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  • 1
    Publication Date: 2011-01-12
    Description: DNA replication fork movement is impeded by collisions with transcription elongation complexes (TEC). We propose that a critical function of transcription termination factors is to prevent TEC from blocking DNA replication and inducing replication fork arrest, one consequence of which is DNA double-strand breaks. We show that inhibition of Rho-dependent transcription termination by bicyclomycin in Escherichia coli induced double-strand breaks. Cells deleted for Rho-cofactors nusA and nusG were hypersensitive to bicyclomycin, and had extensive chromosome fragmentation even in the absence of the drug. An RNA polymerase mutation that destabilizes TEC (rpoB*35) increased bicyclomycin resistance 〉40-fold. Double-strand break formation depended on DNA replication, and can be explained by replication fork collapse. Deleting recombination genes required for replication fork repair (recB and ruvC) increased sensitivity to bicyclomycin, as did loss of the replication fork reloading helicases rep and priA. We propose that Rho responds to a translocating replisome by releasing obstructing TEC.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 2
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    American Association for the Advancement of Science (AAAS)
    In: Science
    Publication Date: 2019
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-03
    Description: Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, S -- Maurizi, M R -- Gottesman, S -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1888-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10583944" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Amyloid/metabolism ; Animals ; Endopeptidases/*metabolism ; Eukaryotic Cells/metabolism ; Humans ; Models, Biological ; Molecular Chaperones/*metabolism ; Prions/metabolism ; Prokaryotic Cells/metabolism ; Protein Biosynthesis ; *Protein Folding ; Proteins/*chemistry/*metabolism ; Ubiquitins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gottesman, S -- Maurizi, M R -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):614-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology and Laboratory of Cell Biology, National Cancer Institute, Bethesda, MD 20892, USA. susang@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11474088" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Dependent Proteases ; Acid Anhydride Hydrolases/metabolism ; Adaptation, Physiological ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acids/*metabolism ; Bacterial Proteins/*metabolism ; Endopeptidase Clp ; Escherichia coli/growth & development/*metabolism ; Guanosine Tetraphosphate/metabolism ; Heat-Shock Proteins/*metabolism ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Polyphosphates/*metabolism ; Ribosomal Proteins/*metabolism ; Serine Endopeptidases/*metabolism ; Ubiquitins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Nature Publishing Group (NPG)
    Publication Date: 2011-04-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gottesman, Susan -- England -- Nature. 2011 Mar 31;471(7340):588-9. doi: 10.1038/471588a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21455171" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/genetics/immunology/metabolism ; Biological Evolution ; DNA, Viral/genetics/metabolism ; Models, Biological ; Plasmids/genetics ; RNA Interference ; RNA Precursors/genetics/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Bacterial/biosynthesis/*genetics/immunology/*metabolism ; RNA, Guide/*genetics ; Ribonuclease III/*metabolism ; Streptococcus pyogenes/*genetics/*immunology/metabolism/virology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2014-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Jiandong -- Gottesman, Susan -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2014 Aug 22;345(6199):876-7. doi: 10.1126/science.1258494.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA. ; Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA. gottesms@helix.nih.gov.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25146272" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cobamides/*metabolism ; Enterococcus faecalis/*genetics ; Ethanolamine/*metabolism ; *Gene Expression Regulation, Bacterial ; Listeria monocytogenes/*genetics ; RNA, Messenger/*metabolism ; RNA, Untranslated/*metabolism ; *Response Elements ; Riboswitch/*physiology ; *Transcription, Genetic ; Vitamin B 12/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 675 (1992), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 596 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 596 (1990), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 773 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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