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Volumn 9, Issue 6, 2006, Pages 612-618

Conditional and replicative senescence in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AGING; ESCHERICHIA COLI; GENE TARGETING; MOLECULAR DYNAMICS; NONHUMAN; OXIDATIVE STRESS; QUALITY CONTROL; REVIEW; SENESCENCE;

EID: 33751253408     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2006.10.010     Document Type: Review
Times cited : (43)

References (43)
  • 1
    • 0035903569 scopus 로고    scopus 로고
    • Bacterial senescence: protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes
    • Ballesteros M., Fredriksson A., Henriksson J., and Nyström T. Bacterial senescence: protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes. EMBO J 18 (2001) 5280-5289
    • (2001) EMBO J , vol.18 , pp. 5280-5289
    • Ballesteros, M.1    Fredriksson, A.2    Henriksson, J.3    Nyström, T.4
  • 3
    • 0025978756 scopus 로고
    • The molecular basis of carbon-starvation-induced general resistance in Escherichia coli
    • Matin A. The molecular basis of carbon-starvation-induced general resistance in Escherichia coli. Mol Microbiol 5 (1991) 3-10
    • (1991) Mol Microbiol , vol.5 , pp. 3-10
    • Matin, A.1
  • 4
    • 0042422247 scopus 로고    scopus 로고
    • The chronological life span of Saccharomyces cerevisiae
    • Fabrizio P., and Longo V.D. The chronological life span of Saccharomyces cerevisiae. Aging Cell 2 (2003) 73-81
    • (2003) Aging Cell , vol.2 , pp. 73-81
    • Fabrizio, P.1    Longo, V.D.2
  • 5
    • 13944272143 scopus 로고    scopus 로고
    • Aging and death in an organism that reproduces by morphologically symmetric division
    • By tracking the poles of cells and measuring growth rate as length increase, the authors observed that the growth rate diminished in cells that inherited old poles. On the basis of these results, the authors suggest that, contrary to previous beliefs, E. coli cells age during exponential growth in a manner that might be similar to replicative aging in the asymmetrically dividing yeasts.
    • Stewart E.J., Madden R., Paul G., and Taddei F. Aging and death in an organism that reproduces by morphologically symmetric division. PLoS Biol 3 (2005) e45. By tracking the poles of cells and measuring growth rate as length increase, the authors observed that the growth rate diminished in cells that inherited old poles. On the basis of these results, the authors suggest that, contrary to previous beliefs, E. coli cells age during exponential growth in a manner that might be similar to replicative aging in the asymmetrically dividing yeasts.
    • (2005) PLoS Biol , vol.3
    • Stewart, E.J.1    Madden, R.2    Paul, G.3    Taddei, F.4
  • 6
    • 0032213238 scopus 로고    scopus 로고
    • Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon
    • Dukan S., and Nyström T. Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev 12 (1998) 3431-3441
    • (1998) Genes Dev , vol.12 , pp. 3431-3441
    • Dukan, S.1    Nyström, T.2
  • 7
    • 0033543618 scopus 로고    scopus 로고
    • Oxidative stress defence and deterioration of growth-arrested Escherichia coli cells
    • Dukan S., and Nyström T. Oxidative stress defence and deterioration of growth-arrested Escherichia coli cells. J Biol Chem 274 (1999) 26027-26032
    • (1999) J Biol Chem , vol.274 , pp. 26027-26032
    • Dukan, S.1    Nyström, T.2
  • 8
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman E.R. Protein oxidation and aging. Science 257 (1992) 1220-1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 9
    • 20444480246 scopus 로고    scopus 로고
    • Defence against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon
    • Fredriksson A., Ballesteros M., Dukan S., and Nyström T. Defence against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol 187 (2005) 4207-4213
    • (2005) J Bacteriol , vol.187 , pp. 4207-4213
    • Fredriksson, A.1    Ballesteros, M.2    Dukan, S.3    Nyström, T.4
  • 10
    • 0037007065 scopus 로고    scopus 로고
    • DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli
    • Echave P., Esparza-Ceron M.A., Cabiscol E., Tamarit J., Ros J., Membrillo-Hernandez J., and Lin E.C. DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli. Proc Natl Acad Sci USA 99 (2002) 4626-4631
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4626-4631
    • Echave, P.1    Esparza-Ceron, M.A.2    Cabiscol, E.3    Tamarit, J.4    Ros, J.5    Membrillo-Hernandez, J.6    Lin, E.C.7
  • 11
    • 0037216549 scopus 로고    scopus 로고
    • Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli
    • Weichart D., Querfurth N., Dreger M., and Hengge-Aronis R. Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J Bacteriol 185 (2003) 115-125
    • (2003) J Bacteriol , vol.185 , pp. 115-125
    • Weichart, D.1    Querfurth, N.2    Dreger, M.3    Hengge-Aronis, R.4
  • 12
    • 0034705167 scopus 로고    scopus 로고
    • Proteins are oxidatively carbonylated in response to reduced transcriptional or translational fidelity
    • Dukan S., Farewell A., Ballestreros M., Taddei F., Radman M., and Nyström T. Proteins are oxidatively carbonylated in response to reduced transcriptional or translational fidelity. Proc Natl Acad Sci USA 97 (2000) 5746-5749
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5746-5749
    • Dukan, S.1    Farewell, A.2    Ballestreros, M.3    Taddei, F.4    Radman, M.5    Nyström, T.6
  • 13
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., and Davies K.J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 4 (2002) 674-680
    • (2002) Nat Cell Biol , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 14
    • 0025633154 scopus 로고
    • Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation
    • Spence J., Cegielska A., and Georgopoulos C. Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation. J Bacteriol 172 (1990) 7157-7166
    • (1990) J Bacteriol , vol.172 , pp. 7157-7166
    • Spence, J.1    Cegielska, A.2    Georgopoulos, C.3
  • 15
    • 9244230099 scopus 로고    scopus 로고
    • Stationary phase physiology
    • Nyström T. Stationary phase physiology. Annu Rev Microbiol 58 (2004) 161-181
    • (2004) Annu Rev Microbiol , vol.58 , pp. 161-181
    • Nyström, T.1
  • 16
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nyström T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 24 (2005) 1311-1317
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nyström, T.1
  • 17
    • 0038779369 scopus 로고    scopus 로고
    • Differential oxidative damage and expression of stress regulons in culturable and nonculturable cells of Escherichia coli
    • Desnues B., Gregori G., Dukan S., Aguilaniu H., and Nyström T. Differential oxidative damage and expression of stress regulons in culturable and nonculturable cells of Escherichia coli. EMBO Rep 4 (2003) 400-405
    • (2003) EMBO Rep , vol.4 , pp. 400-405
    • Desnues, B.1    Gregori, G.2    Dukan, S.3    Aguilaniu, H.4    Nyström, T.5
  • 18
    • 0038687689 scopus 로고    scopus 로고
    • The Ras and Sch9 pathways regulate stress resistance and longevity
    • Longo V.D. The Ras and Sch9 pathways regulate stress resistance and longevity. Exp Gerontol 38 (2003) 807-811
    • (2003) Exp Gerontol , vol.38 , pp. 807-811
    • Longo, V.D.1
  • 19
    • 0037683664 scopus 로고    scopus 로고
    • Mnsod overexpression extends the yeast chronological (G(0)) life span but acts independently of Sir2p histone deacetylase to shorten the replicative life span of dividing cells
    • Harris N., Costa V., MacLean M., Mollapour M., Moradas-Ferreira P., and Piper P.W. Mnsod overexpression extends the yeast chronological (G(0)) life span but acts independently of Sir2p histone deacetylase to shorten the replicative life span of dividing cells. Free Radic Biol Med 3412 (2003) 1599-1606
    • (2003) Free Radic Biol Med , vol.3412 , pp. 1599-1606
    • Harris, N.1    Costa, V.2    MacLean, M.3    Mollapour, M.4    Moradas-Ferreira, P.5    Piper, P.W.6
  • 21
    • 0038263852 scopus 로고    scopus 로고
    • val19 allele elevates ROS production and locks mitochondrial respiration in a non-phosphorylating mode independently of the PKA pathway
    • val19 allele elevates ROS production and locks mitochondrial respiration in a non-phosphorylating mode independently of the PKA pathway. EMBO J 22 (2003) 3337-3345
    • (2003) EMBO J , vol.22 , pp. 3337-3345
    • Hlavata, L.1    Aguilaniu, H.2    Pichova, A.3    Nyström, T.4
  • 22
    • 24944557141 scopus 로고    scopus 로고
    • Differential roles of the universal stress proteins in oxidative stress resistance, adhesion, and motility
    • Nachin L., Nannmark U., and Nyström T. Differential roles of the universal stress proteins in oxidative stress resistance, adhesion, and motility. J Bacteriol 187 (2005) 6265-6272
    • (2005) J Bacteriol , vol.187 , pp. 6265-6272
    • Nachin, L.1    Nannmark, U.2    Nyström, T.3
  • 23
    • 0038013951 scopus 로고    scopus 로고
    • Bacterial universal stress proteins: function and regulation
    • Kvint K., Nachin L., Diez A., and Nyström T. Bacterial universal stress proteins: function and regulation. Curr Opin Microbiol 6 (2003) 140-145
    • (2003) Curr Opin Microbiol , vol.6 , pp. 140-145
    • Kvint, K.1    Nachin, L.2    Diez, A.3    Nyström, T.4
  • 24
    • 33645086142 scopus 로고    scopus 로고
    • Induction of the heat shock regulon in response to increased mistranslation requires the presence of oxygen
    • Fredriksson A., Ballesteros M., Dukan S., and Nyström T. Induction of the heat shock regulon in response to increased mistranslation requires the presence of oxygen. Mol Microbiol 59 (2006) 350-359
    • (2006) Mol Microbiol , vol.59 , pp. 350-359
    • Fredriksson, A.1    Ballesteros, M.2    Dukan, S.3    Nyström, T.4
  • 25
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • This paper shows that upon exposure of cells to reactive oxygen species and elevated temperatures, the DnaK chaperone system fails to function. Inactivation of DnaK is argued to result from a dramatic decrease in intracellular ATP levels, rendering the ATPase domain of DnaK nucleotide depleted and thermolabile.
    • Winter J., Linke K., Jatzek A., and Jakob U. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol Cell 17 (2005) 381-392. This paper shows that upon exposure of cells to reactive oxygen species and elevated temperatures, the DnaK chaperone system fails to function. Inactivation of DnaK is argued to result from a dramatic decrease in intracellular ATP levels, rendering the ATPase domain of DnaK nucleotide depleted and thermolabile.
    • (2005) Mol Cell , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 26
    • 0036714331 scopus 로고    scopus 로고
    • Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase
    • Hengge-Aronis R. Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase. Microbiol Mol Biol Rev 66 (2002) 373-395
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 373-395
    • Hengge-Aronis, R.1
  • 27
    • 0034002888 scopus 로고    scopus 로고
    • Regulation of sigma S degradation in Salmonella enterica var Typhimurium: in vivo interactions between sigma S, the response regulator MviA(RssB) and ClpX
    • Moreno M., Audia J.P., Bearson S.M., Webb C., and Foster J.W. Regulation of sigma S degradation in Salmonella enterica var Typhimurium: in vivo interactions between sigma S, the response regulator MviA(RssB) and ClpX. J Mol Microbiol Biotechnol 2 (2000) 245-254
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 245-254
    • Moreno, M.1    Audia, J.P.2    Bearson, S.M.3    Webb, C.4    Foster, J.W.5
  • 28
    • 0034933066 scopus 로고    scopus 로고
    • Role of the response regulator RssB in sigma recognition and initiation of sigma proteolysis in Escherichia coli
    • Klauck E., Lingnau M., and Hengge-Aronis R. Role of the response regulator RssB in sigma recognition and initiation of sigma proteolysis in Escherichia coli. Mol Microbiol 40 (2001) 1381-1390
    • (2001) Mol Microbiol , vol.40 , pp. 1381-1390
    • Klauck, E.1    Lingnau, M.2    Hengge-Aronis, R.3
  • 29
    • 27744589294 scopus 로고    scopus 로고
    • A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli
    • Mika F., and Hengge R. A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli. Genes Dev 19 (2005) 2770-2781
    • (2005) Genes Dev , vol.19 , pp. 2770-2781
    • Mika, F.1    Hengge, R.2
  • 30
    • 6044235523 scopus 로고    scopus 로고
    • RpoS proteolysis is regulated by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site
    • Peterson C.N., Ruiz N., and Silhavy T.J. RpoS proteolysis is regulated by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site. J Bacteriol 186 (2004) 7403-7410
    • (2004) J Bacteriol , vol.186 , pp. 7403-7410
    • Peterson, C.N.1    Ruiz, N.2    Silhavy, T.J.3
  • 31
    • 33645522854 scopus 로고    scopus 로고
    • Modulating RssB activity: IraP, a novel regulator of sigma(S) stability in Escherichia coli
    • Bougdour A., Wickner S., and Gottesman S. Modulating RssB activity: IraP, a novel regulator of sigma(S) stability in Escherichia coli. Genes Dev 20 (2006) 884-897
    • (2006) Genes Dev , vol.20 , pp. 884-897
    • Bougdour, A.1    Wickner, S.2    Gottesman, S.3
  • 32
    • 11844276053 scopus 로고    scopus 로고
    • Starvation for different nutrients in Escherichia coli results in differential modulation of RpoS levels and stability
    • Mandel M.J., and Silhavy T.J. Starvation for different nutrients in Escherichia coli results in differential modulation of RpoS levels and stability. J Bacteriol 187 (2005) 434-442
    • (2005) J Bacteriol , vol.187 , pp. 434-442
    • Mandel, M.J.1    Silhavy, T.J.2
  • 33
    • 0037470539 scopus 로고    scopus 로고
    • Genetics and the specificity of the aging process
    • Hekimi S., and Guarente L. Genetics and the specificity of the aging process. Science 299 (2003) 1351-1354
    • (2003) Science , vol.299 , pp. 1351-1354
    • Hekimi, S.1    Guarente, L.2
  • 34
    • 0038724020 scopus 로고    scopus 로고
    • Senescence in a bacterium with asymmetric division
    • Ackermann M., Stearns S.C., and Jenal U. Senescence in a bacterium with asymmetric division. Science 300 (2003) 1920
    • (2003) Science , vol.300 , pp. 1920
    • Ackermann, M.1    Stearns, S.C.2    Jenal, U.3
  • 35
    • 0032861978 scopus 로고    scopus 로고
    • Replicative ageing in the fission yeast Schizosaccharomyces pombe
    • Barker M.G., and Walmsley R.M. Replicative ageing in the fission yeast Schizosaccharomyces pombe. Yeast 15 (1999) 1511-1518
    • (1999) Yeast , vol.15 , pp. 1511-1518
    • Barker, M.G.1    Walmsley, R.M.2
  • 36
    • 26244455975 scopus 로고    scopus 로고
    • Aging in Escherichia coli: signals in the noise
    • Stewart E., and Taddei F. Aging in Escherichia coli: signals in the noise. Bioessays 27 (2005) 983
    • (2005) Bioessays , vol.27 , pp. 983
    • Stewart, E.1    Taddei, F.2
  • 37
    • 24644468691 scopus 로고    scopus 로고
    • Is Escherichia coli getting old?
    • Woldringh C.L. Is Escherichia coli getting old?. Bioessays 27 (2005) 770-774
    • (2005) Bioessays , vol.27 , pp. 770-774
    • Woldringh, C.L.1
  • 38
    • 20544464210 scopus 로고    scopus 로고
    • Replicative aging in E. coli
    • Lynch M.D. Replicative aging in E. coli. Rejuvenation Res 8 (2005) 79-81
    • (2005) Rejuvenation Res , vol.8 , pp. 79-81
    • Lynch, M.D.1
  • 39
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis in Saccharomyces cerevisiae: a Sir2p dependent mechanism
    • Aguilaniu H., Gustafsson L., Rigoulet M., and Nyström T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis in Saccharomyces cerevisiae: a Sir2p dependent mechanism. Science 299 (2003) 1751-1753
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nyström, T.4
  • 40
    • 16244399543 scopus 로고    scopus 로고
    • Asymmetry and the origins of ageing
    • Kirkwood T.B. Asymmetry and the origins of ageing. Mech Ageing Dev 126 (2005) 533-534
    • (2005) Mech Ageing Dev , vol.126 , pp. 533-534
    • Kirkwood, T.B.1
  • 41
    • 13944269223 scopus 로고    scopus 로고
    • The plasticity of aging: insights from long-lived mutants
    • Kenyon C. The plasticity of aging: insights from long-lived mutants. Cell 120 (2005) 449-460
    • (2005) Cell , vol.120 , pp. 449-460
    • Kenyon, C.1
  • 42
    • 0041867968 scopus 로고    scopus 로고
    • The free radical hypothesis of aging goes prokaryotic
    • Nyström T. The free radical hypothesis of aging goes prokaryotic. Cell Mol Life Sci 60 (2003) 1333-1341
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1333-1341
    • Nyström, T.1
  • 43
    • 33646744719 scopus 로고    scopus 로고
    • Elimination of damaged proteins during differentiation of embryonic stem cells
    • These authors demonstrate that undifferentiated mouse ES cells and cells of the inner cell-mass of blastocysts, unexpectedly contain high levels of damaged proteins. This damage is rapidly eliminated upon differentiation of ES cells in vitro and during normal embryonic development in vivo. These results might call for re-evaluation of the notion that the offspring of mammals start out with low levels of (cytosolic) damage because of a mechanism that keeps the germ-line cells free of deteriorated macromolecules.
    • Hernebring M., Brolén G., Aguilaniu H., Semb H., and Nyström T. Elimination of damaged proteins during differentiation of embryonic stem cells. Proc Natl Acad Sci USA 103 (2006) 7700-7705. These authors demonstrate that undifferentiated mouse ES cells and cells of the inner cell-mass of blastocysts, unexpectedly contain high levels of damaged proteins. This damage is rapidly eliminated upon differentiation of ES cells in vitro and during normal embryonic development in vivo. These results might call for re-evaluation of the notion that the offspring of mammals start out with low levels of (cytosolic) damage because of a mechanism that keeps the germ-line cells free of deteriorated macromolecules.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7700-7705
    • Hernebring, M.1    Brolén, G.2    Aguilaniu, H.3    Semb, H.4    Nyström, T.5


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