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Functions of typical 2-Cys peroxiredoxins in yeast

Lookup NU author(s): Professor Brian Morgan, Dr Elizabeth Veal


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Peroxiredoxins are ubiquitous proteins that are found from bacteria to humans. Until recently they were thought to solely act as antioxidants catalysing the reduction of peroxides through their associated thioredoxin peroxidase activity. However, recent work has begun to uncover hitherto unsuspected roles for one group of these proteins, the typical 2-Cys peroxiredoxins (2-Cys Prx). For example, typical 2-Cys Prxs have been found to have roles in the model organisms Schizosaccharomvces pombe and Saccharomyces cerevisiae in regulating signal transduction, in DNA damage responses and as molecular chaperones. There is increasing evidence that H2O2 is utilised as a signalling molecule to regulate a range of important cellular processes. As abundant and ubiquitous peroxidase enzymes the peroxidase activity of typical 2-Cys Prxs is important in the regulation of these functions. Significantly, studies in yeast suggest that the regulation of the thioredoxin peroxidase and chaperone activities of these multifunction enzymes is an important aspect of H2O2-mediated signal transduction and consequently have provided important insight into the roles of these proteins in higher eukaryotes.

Publication metadata

Author(s): Morgan BA, Veal EA

Publication type: Article

Publication status: Published

Journal: SubCellular Biochemistry

Year: 2007

Volume: 44

Pages: 253-65

ISSN (print): 0306-0225

Publisher: Springer New York LLC


DOI: 10.1007/978-1-4020-6051-9_12

Notes: Journal Article Research Support, Non-U.S. Gov't Review England


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