Show simple item record

Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae

dc.contributor.authorWholey, Wei‐yunen_US
dc.contributor.authorJakob, Ursulaen_US
dc.date.accessioned2012-03-16T15:54:53Z
dc.date.available2013-05-01T17:24:42Zen_US
dc.date.issued2012-03en_US
dc.identifier.citationWholey, 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.issn0950-382Xen_US
dc.identifier.issn1365-2958en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/90122
dc.publisherBlackwell Publishing Ltden_US
dc.publisherWiley Periodicals, Inc.en_US
dc.titleHsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio choleraeen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumCellular and Molecular Biology Program, University of Michigan Medical School, Ann Arbor, MI 48109, USA.en_US
dc.contributor.affiliationumDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.en_US
dc.identifier.pmid22296329en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90122/1/j.1365-2958.2012.07982.x.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90122/2/MMI_7982_sm_FigS1-S5.pdf
dc.identifier.doi10.1111/j.1365-2958.2012.07982.xen_US
dc.identifier.sourceMolecular Microbiologyen_US
dc.identifier.citedreferenceCaldas, 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.citedreferenceDefeu 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.citedreferenceFurano, A.V. ( 1975 ) Content of elongation factor Tu in Escherichia coli. Proc Natl Acad Sci USA 72: 4780 – 4784.en_US
dc.identifier.citedreferenceHyslop, 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.citedreferenceIlbert, 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.citedreferenceKudlicki, 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.citedreferenceLeichert, L.I., and Jakob, U. ( 2004 ) Protein thiol modifications visualized in vivo. PLoS Biol 2: e333.en_US
dc.identifier.citedreferenceLeichert, 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.citedreferenceLuo, S., and Levine, R.L. ( 2009 ) Methionine in proteins defends against oxidative stress. FASEB J 23: 464 – 472.en_US
dc.identifier.citedreferenceMiller, R.A., and Britigan, B.E. ( 1997 ) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1 – 18.en_US
dc.identifier.citedreferencePedersen, 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.citedreferenceThompson, 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.citedreferenceWeijland, 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.citedreferenceWinter, 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.citedreferenceWinter, 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.citedreferenceZander, T., Phadke, N.D., and Bardwell, J.C. ( 1998 ) Disulfide bond catalysts in Escherichia coli. Methods Enzymol 290: 59 – 74.en_US
dc.identifier.citedreferenceZengel, 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.citedreferenceBeck, B.D. ( 1979 ) Polymerization of the bacterial elongation factor for protein synthesis, EF‐Tu. Eur J Biochem 97: 495 – 502.en_US
dc.identifier.citedreferenceButland, 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.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.