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Phagocytic cells inhibit the growth of intracellular pathogens by producing nitric oxide (NO). NO causes cell filamentation, induction of the SOS response, and DNA replication arrest in the Gram-negative bacterium Salmonella enterica. NO also induces double-stranded chromosomal breaks in replication-arrested Salmonella lacking a functional RecBCD exonuclease. This DNA damage depends on actions of additional DNA repair proteins, the RecG helicase, and RuvC endonuclease. Introduction of a recG mutation restores both resistance to NO and the ability of an attenuated recBC mutant Salmonella strain to cause lethal infection in mice, demonstrating that bacterial DNA replication is inhibited during host-pathogen interactions. Inhibition of DNA replication during nitrosative stress is invariably accompanied by zinc mobilization, implicating DNA-binding zinc metalloproteins as critical targets of NO-related antimicrobial activity.

Titel:	Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress.
Autor/in / Beteiligte Person:	Schapiro, JM ; Libby, SJ ; Fang, FC
Link:	Full Text Finder (Volltext)
Zeitschrift:	Proceedings of the National Academy of Sciences of the United States of America, Jg. 100 (2003-07-08), Heft 14, S. 8496-501
Veröffentlichung:	Washington, DC : National Academy of Sciences, 2003
Medientyp:	academicJournal
ISSN:	0027-8424 (print)
DOI:	10.1073/pnas.1033133100
Schlagwort:	Animals Bacterial Proteins genetics Chromosome Breakage Chromosomes, Bacterial genetics DNA Damage DNA Helicases deficiency DNA Helicases genetics DNA Helicases metabolism DNA Repair Endodeoxyribonucleases deficiency Endodeoxyribonucleases genetics Endodeoxyribonucleases metabolism Exodeoxyribonuclease V Exodeoxyribonucleases deficiency Exodeoxyribonucleases genetics Exodeoxyribonucleases metabolism Membrane Glycoproteins deficiency Membrane Glycoproteins genetics Membrane Glycoproteins metabolism Mice Mice, Inbred C57BL NADPH Oxidase 2 Nitric Oxide Synthase deficiency Nitric Oxide Synthase genetics Nitric Oxide Synthase metabolism Nitric Oxide Synthase Type II S-Nitrosothiols metabolism Salmonella enterica metabolism Bacterial Proteins metabolism DNA Replication DNA, Bacterial biosynthesis Escherichia coli Proteins NADPH Oxidases Nitric Oxide physiology Phagocytosis physiology Salmonella enterica genetics Zinc metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. Language: English [Proc Natl Acad Sci U S A] 2003 Jul 08; Vol. 100 (14), pp. 8496-501. <i>Date of Electronic Publication: </i>2003 Jun 26. MeSH Terms: DNA Replication* ; Escherichia coli Proteins* ; NADPH Oxidases* ; Bacterial Proteins / metabolism ; DNA, Bacterial / biosynthesis ; Nitric Oxide / physiology ; Phagocytosis / physiology ; Salmonella enterica / genetics ; Zinc / metabolism ; Animals ; Bacterial Proteins / genetics ; Chromosome Breakage ; Chromosomes, Bacterial / genetics ; DNA Damage ; DNA Helicases / deficiency ; DNA Helicases / genetics ; DNA Helicases / metabolism ; DNA Repair ; Endodeoxyribonucleases / deficiency ; Endodeoxyribonucleases / genetics ; Endodeoxyribonucleases / metabolism ; Exodeoxyribonuclease V ; Exodeoxyribonucleases / deficiency ; Exodeoxyribonucleases / genetics ; Exodeoxyribonucleases / metabolism ; Membrane Glycoproteins / deficiency ; Membrane Glycoproteins / genetics ; Membrane Glycoproteins / metabolism ; Mice ; Mice, Inbred C57BL ; NADPH Oxidase 2 ; Nitric Oxide Synthase / deficiency ; Nitric Oxide Synthase / genetics ; Nitric Oxide Synthase / metabolism ; Nitric Oxide Synthase Type II ; S-Nitrosothiols / metabolism ; Salmonella enterica / metabolism References: Mol Med. 1999 Nov;5(11):721-30. (PMID: 10656874) ; FEBS Lett. 1999 Jul 9;454(3):177-80. (PMID: 10431802) ; J Exp Med. 2000 Jul 17;192(2):227-36. (PMID: 10899909) ; J Exp Med. 2000 Jul 17;192(2):237-48. (PMID: 10899910) ; FASEB J. 2000 Oct;14(13):1889-900. (PMID: 11023973) ; J Bacteriol. 2001 Jan;183(1):131-8. (PMID: 11114909) ; Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8235-40. (PMID: 11459958) ; Cell. 2001 Sep 21;106(6):675-83. (PMID: 11572774) ; J Bacteriol. 2002 Jan;184(2):592-5. (PMID: 11751841) ; Mol Microbiol. 2002 Feb;43(3):771-82. (PMID: 11929531) ; J Bacteriol. 2002 Jul;184(13):3501-7. (PMID: 12057944) ; J Biol Chem. 2002 Nov 15;277(46):44327-31. (PMID: 12213816) ; J Bacteriol. 1979 Apr;138(1):105-8. (PMID: 374357) ; Cell. 1982 May;29(1):11-22. (PMID: 7049397) ; Science. 1988 Apr 29;240(4852):640-2. (PMID: 2834821) ; J Photochem Photobiol B. 1987 Sep;1(1):1-11. (PMID: 3149975) ; J Bacteriol. 1989 Nov;171(11):6141-7. (PMID: 2681154) ; J Mol Biol. 1990 Mar 5;212(1):79-96. (PMID: 2108251) ; Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3029-32. (PMID: 1826559) ; J Bacteriol. 1991 Nov;173(21):6686-93. (PMID: 1938875) ; Science. 1991 Nov 15;254(5034):1001-3. (PMID: 1948068) ; Microbiol Rev. 1991 Dec;55(4):561-85. (PMID: 1779927) ; Mol Microbiol. 1992 Oct;6(19):2755-9. (PMID: 1435254) ; Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11978-82. (PMID: 1465428) ; Science. 1992 Dec 18;258(5090):1898-902. (PMID: 1281928) ; Mol Microbiol. 1993 Mar;7(6):933-6. (PMID: 8387147) ; Carcinogenesis. 1994 Mar;15(3):443-7. (PMID: 8118926) ; Biochem Biophys Res Commun. 1994 Apr 29;200(2):1105-10. (PMID: 8179589) ; Cell. 1994 Sep 23;78(6):931-6. (PMID: 7923362) ; Microbiol Rev. 1994 Sep;58(3):401-65. (PMID: 7968921) ; Nucleic Acids Res. 1994 Dec 11;22(24):5366-70. (PMID: 7816627) ; J Clin Invest. 1995 Mar;95(3):1047-53. (PMID: 7883952) ; Biochem Biophys Res Commun. 1995 Apr 6;209(1):198-204. (PMID: 7726836) ; Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6399-403. (PMID: 7604003) ; Chem Res Toxicol. 1995 Apr-May;8(3):473-7. (PMID: 7578935) ; Clin Infect Dis. 1995 Oct;21 Suppl 2:S162-5. (PMID: 8845445) ; Mol Microbiol. 1995 Sep;17(6):1177-88. (PMID: 8594336) ; Mutat Res. 1996 Jan 17;349(1):51-61. (PMID: 8569792) ; J Bacteriol. 1996 Mar;178(5):1258-64. (PMID: 8631700) ; Mol Microbiol. 1996 Feb;19(4):871-80. (PMID: 8820655) ; Carcinogenesis. 1996 Nov;17(11):2501-5. (PMID: 8968069) ; EMBO J. 1997 Jan 15;16(2):430-8. (PMID: 9029161) ; Microbiology. 1997 Feb;143 ( Pt 2):585-94. (PMID: 9043135) ; Neuron. 1997 May;18(5):691-6. (PMID: 9182795) ; Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13997-4001. (PMID: 9391141) ; Cell. 1998 Oct 30;95(3):419-30. (PMID: 9814711) ; Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3552-5. (PMID: 10097074) ; Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6640-5. (PMID: 10829079) Substance Nomenclature: 0 (Bacterial Proteins) ; 0 (DNA, Bacterial) ; 0 (Escherichia coli Proteins) ; 0 (Membrane Glycoproteins) ; 0 (S-Nitrosothiols) ; 31C4KY9ESH (Nitric Oxide) ; EC 1.14.13.39 (Nitric Oxide Synthase) ; EC 1.14.13.39 (Nitric Oxide Synthase Type II) ; EC 1.14.13.39 (Nos2 protein, mouse) ; EC 1.6.3.- (CYBB protein, human) ; EC 1.6.3.- (NADPH Oxidase 2) ; EC 1.6.3.- (NADPH Oxidases) ; EC 3.1.- (Endodeoxyribonucleases) ; EC 3.1.- (Exodeoxyribonucleases) ; EC 3.1.11.5 (Exodeoxyribonuclease V) ; EC 3.1.11.5 (exodeoxyribonuclease V, E coli) ; EC 3.6.4.- (DNA Helicases) ; J41CSQ7QDS (Zinc) Entry Date(s): Date Created: 20030628 Date Completed: 20030904 Latest Revision: 20181113 Update Code: 20240513 PubMed Central ID: PMC166257

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Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress.