Redox-regulated molecular chaperones
dc.contributor.author | Jakob, Ursula | en_US |
dc.contributor.author | Graf, Paul C. F. | en_US |
dc.date.accessioned | 2006-09-08T19:41:15Z | |
dc.date.available | 2006-09-08T19:41:15Z | |
dc.date.issued | 2002-10 | en_US |
dc.identifier.citation | Graf, P. C. F.; Jakob, U.; (2002). "Redox-regulated molecular chaperones." Cellular and Molecular Life Sciences 59(10): 1624-1631. <http://hdl.handle.net/2027.42/41834> | en_US |
dc.identifier.issn | 1420-682X | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/41834 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12475172&dopt=citation | en_US |
dc.description.abstract | The conserved heat shock protein Hsp33 functions as a potent molecular chaperone with a highly sophisticated regulation. On transcriptional level, the Hsp33 gene is under heat shock control; on posttranslational level, the Hsp33 protein is under oxidative stress control. This dual regulation appears to reflect the close but rather neglected connection between heat shock and oxidative stress. The redox sensor in Hsp33 is a cysteine center that coordinates zinc under reducing, inactivating conditions and that forms two intramolecular disulfide bonds under oxidizing, activating conditions. Hsp33's redox-regulated chaperone activity appears to specifically protect proteins and cells from the otherwise deleterious effects of reactive oxygen species. That redox regulation of chaperone activity is not restricted to Hsp33 became evident when the chaperone activity of protein disulfide isomerase was recently also shown to cycle between a low- and high-affinity substrate binding state, depending on the redox state of its cysteines. | en_US |
dc.format.extent | 171769 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Birkhäuser Verlag; Springer Science+Business Media | en_US |
dc.subject.other | Legacy | en_US |
dc.subject.other | Key Words. Hsp33; PDI; Redox Regulation; Disulfide Bond Formation; Oxidative Stress; Heat Shock; Metal Centers; Reactive Oxygen Species. | en_US |
dc.title | Redox-regulated molecular chaperones | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Science (General) | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, Michigan 48109-1048 (USA), US | en_US |
dc.contributor.affiliationum | Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University Avenue, Ann Arbor, Michigan 48109-1048 (USA), Fax +1 734 647 0884, e-mail: ujakob@umich.edu, US | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 12475172 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/41834/1/20591624.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/PL00012489 | en_US |
dc.identifier.source | Cellular and Molecular Life Sciences | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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