Stress induction and mitochondrial localization of Oxr1 proteins in yeast and humans
dc.contributor.author | Elliott, Nathan Andrew | |
dc.contributor.author | Volkert, Michael R. | |
dc.date | 2022-08-11T08:08:57.000 | |
dc.date.accessioned | 2022-08-23T16:13:39Z | |
dc.date.available | 2022-08-23T16:13:39Z | |
dc.date.issued | 2004-04-03 | |
dc.date.submitted | 2008-09-04 | |
dc.identifier.citation | <p>Mol Cell Biol. 2004 Apr;24(8):3180-7.</p> | |
dc.identifier.issn | 0270-7306 (Print) | |
dc.identifier.doi | 10.1128/MCB.24.8.3180-3187.2004 | |
dc.identifier.pmid | 15060142 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/33674 | |
dc.description.abstract | Reactive oxygen species (ROS) are critical molecules produced as a consequence of aerobic respiration. It is essential for cells to control the production and activity of such molecules in order to protect the genome and regulate cellular processes such as stress response and apoptosis. Mitochondria are the major source of ROS within the cell, and as a result, numerous proteins have evolved to prevent or repair oxidative damage in this organelle. The recently discovered OXR1 gene family represents a set of conserved eukaryotic genes. Previous studies of the yeast OXR1 gene indicate that it functions to protect cells from oxidative damage. In this report, we show that human and yeast OXR1 genes are induced by heat and oxidative stress and that their proteins localize to the mitochondria and function to protect against oxidative damage. We also demonstrate that mitochondrial localization is required for Oxr1 protein to prevent oxidative damage. | |
dc.language.iso | en_US | |
dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15060142&dopt=Abstract">Link to article in PubMed</a></p> | |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC381681/ | |
dc.subject | *Gene Expression Regulation; Genetic Complementation Test; Heat; Hela Cells; Humans; Hydrogen Peroxide; Mitochondria; Oxidants; Oxidation-Reduction; Oxidative Stress; Proteins; Reactive Oxygen Species; Saccharomyces cerevisiae; Tissue Distribution | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Stress induction and mitochondrial localization of Oxr1 proteins in yeast and humans | |
dc.type | Journal Article | |
dc.source.journaltitle | Molecular and cellular biology | |
dc.source.volume | 24 | |
dc.source.issue | 8 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/339 | |
dc.identifier.contextkey | 619051 | |
html.description.abstract | <p>Reactive oxygen species (ROS) are critical molecules produced as a consequence of aerobic respiration. It is essential for cells to control the production and activity of such molecules in order to protect the genome and regulate cellular processes such as stress response and apoptosis. Mitochondria are the major source of ROS within the cell, and as a result, numerous proteins have evolved to prevent or repair oxidative damage in this organelle. The recently discovered OXR1 gene family represents a set of conserved eukaryotic genes. Previous studies of the yeast OXR1 gene indicate that it functions to protect cells from oxidative damage. In this report, we show that human and yeast OXR1 genes are induced by heat and oxidative stress and that their proteins localize to the mitochondria and function to protect against oxidative damage. We also demonstrate that mitochondrial localization is required for Oxr1 protein to prevent oxidative damage.</p> | |
dc.identifier.submissionpath | gsbs_sp/339 | |
dc.contributor.department | Department of Molecular Genetics and Microbiology | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 3180-7 |