Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae
dc.contributor.author | Wholey, Wei‐yun | en_US |
dc.contributor.author | Jakob, Ursula | en_US |
dc.date.accessioned | 2012-03-16T15:54:53Z | |
dc.date.available | 2013-05-01T17:24:42Z | en_US |
dc.date.issued | 2012-03 | en_US |
dc.identifier.citation | Wholey, Wei‐yun ; Jakob, Ursula (2012). "Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae ." Molecular Microbiology 83(5). <http://hdl.handle.net/2027.42/90122> | en_US |
dc.identifier.issn | 0950-382X | en_US |
dc.identifier.issn | 1365-2958 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/90122 | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.publisher | Wiley Periodicals, Inc. | en_US |
dc.title | Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Microbiology and Immunology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Cellular and Molecular Biology Program, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | en_US |
dc.contributor.affiliationum | Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA. | en_US |
dc.identifier.pmid | 22296329 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/90122/1/j.1365-2958.2012.07982.x.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/90122/2/MMI_7982_sm_FigS1-S5.pdf | |
dc.identifier.doi | 10.1111/j.1365-2958.2012.07982.x | en_US |
dc.identifier.source | Molecular Microbiology | en_US |
dc.identifier.citedreference | Caldas, T.D., El Yaagoubi, A., and Richarme, G. ( 1998 ) Chaperone properties of bacterial elongation factor EF‐Tu. J Biol Chem 273: 11478 – 11482. | en_US |
dc.identifier.citedreference | Defeu Soufo, H.J., Reimold, C., Linne, U., Knust, T., Gescher, J., and Graumann, P.L. ( 2010 ) Bacterial translation elongation factor EF‐Tu interacts and colocalizes with actin‐like MreB protein. Proc Natl Acad Sci USA 107: 3163 – 3168. | en_US |
dc.identifier.citedreference | Furano, A.V. ( 1975 ) Content of elongation factor Tu in Escherichia coli. Proc Natl Acad Sci USA 72: 4780 – 4784. | en_US |
dc.identifier.citedreference | Hyslop, P.A., Hinshaw, D.B., Halsey, W.A., Jr, Schraufstatter, I.U., Sauerheber, R.D., Spragg, R.G., et al.( 1988 ) Mechanisms of oxidant‐mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J Biol Chem 263: 1665 – 1675. | en_US |
dc.identifier.citedreference | Ilbert, M., Horst, J., Ahrens, S., Winter, J., Graf, P.C., Lilie, H., and Jakob, U. ( 2007 ) The redox‐switch domain of Hsp33 functions as dual stress sensor. Nat Struct Mol Biol 14: 556 – 563. | en_US |
dc.identifier.citedreference | Kudlicki, W., Coffman, A., Kramer, G., and Hardesty, B. ( 1997 ) Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF‐Tu flexing. J Biol Chem 272: 32206 – 32210. | en_US |
dc.identifier.citedreference | Leichert, L.I., and Jakob, U. ( 2004 ) Protein thiol modifications visualized in vivo. PLoS Biol 2: e333. | en_US |
dc.identifier.citedreference | Leichert, L.I., Gehrke, F., Gudiseva, H.V., Blackwell, T., Ilbert, M., Walker, A.K., et al. ( 2008 ) Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc Natl Acad Sci USA 105: 8197 – 8202. | en_US |
dc.identifier.citedreference | Luo, S., and Levine, R.L. ( 2009 ) Methionine in proteins defends against oxidative stress. FASEB J 23: 464 – 472. | en_US |
dc.identifier.citedreference | Miller, R.A., and Britigan, B.E. ( 1997 ) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1 – 18. | en_US |
dc.identifier.citedreference | Pedersen, S., Bloch, P.L., Reeh, S., and Neidhardt, F.C. ( 1978 ) Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell 14: 179 – 190. | en_US |
dc.identifier.citedreference | Thompson, R.C., Dix, D.B., and Karim, A.M. ( 1986 ) The reaction of ribosomes with elongation factor Tu.GTP complexes. Aminoacyl‐tRNA‐independent reactions in the elongation cycle determine the accuracy of protein synthesis. J Biol Chem 261: 4868 – 4874. | en_US |
dc.identifier.citedreference | Weijland, A., and Parmeggiani, A. ( 1994 ) Why do two EF‐Tu molecules act in the elongation cycle of protein biosynthesis? Trends Biochem Sci 19: 188 – 193. | en_US |
dc.identifier.citedreference | Winter, J., Linke, K., Jatzek, A., and Jakob, U. ( 2005 ) Severe oxidative stress causes inactivation of DnaK and activation of the redox‐regulated chaperone Hsp33. Mol Cell 17: 381 – 392. | en_US |
dc.identifier.citedreference | Winter, J., Ilbert, M., Graf, P.C., Ozcelik, D., and Jakob, U. ( 2008 ) Bleach activates a redox‐regulated chaperone by oxidative protein unfolding. Cell 135: 691 – 701. | en_US |
dc.identifier.citedreference | Zander, T., Phadke, N.D., and Bardwell, J.C. ( 1998 ) Disulfide bond catalysts in Escherichia coli. Methods Enzymol 290: 59 – 74. | en_US |
dc.identifier.citedreference | Zengel, J.M., and Lindahl, L. ( 1990 ) Mapping of two promoters for elongation factor Tu within the structural gene for elongation factor G. Biochim Biophys Acta 1050: 317 – 322. | en_US |
dc.identifier.citedreference | Beck, B.D. ( 1979 ) Polymerization of the bacterial elongation factor for protein synthesis, EF‐Tu. Eur J Biochem 97: 495 – 502. | en_US |
dc.identifier.citedreference | Butland, G., Peregrin‐Alvarez, J.M., Li, J., Yang, W., Yang, X., Canadien, V., et al. ( 2005 ) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531 – 537. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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