Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman

Oxidative proteome damage has been implicated as a major contributor to cell death and aging. Protein damage and aging has been a particular theme of the recent research of Miroslav Radman. However, the study of how cellular proteins are damaged by oxidative processes is still in its infancy. Here w...

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Main Authors: Steven T. Bruckbauer, Benjamin B. Minkoff, Michael R. Sussman, Michael M. Cox
Format: Article
Language:English
Published: MDPI AG 2021-04-01
Series:Cells
Subjects:
Online Access:https://www.mdpi.com/2073-4409/10/4/954
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author Steven T. Bruckbauer
Benjamin B. Minkoff
Michael R. Sussman
Michael M. Cox
author_facet Steven T. Bruckbauer
Benjamin B. Minkoff
Michael R. Sussman
Michael M. Cox
author_sort Steven T. Bruckbauer
collection DOAJ
description Oxidative proteome damage has been implicated as a major contributor to cell death and aging. Protein damage and aging has been a particular theme of the recent research of Miroslav Radman. However, the study of how cellular proteins are damaged by oxidative processes is still in its infancy. Here we examine oxidative changes in the proteomes of four bacterial populations—wild type <i>E. coli</i>, two isolates from <i>E. coli</i> populations evolved for high levels of ionizing radiation (IR) resistance, and <i>D. radiodurans</i>—immediately following exposure to 3000 Gy of ionizing radiation. By a substantial margin, the most prominent intracellular oxidation events involve hydroxylation of methionine residues. Significant but much less frequent are carbonylation events on tyrosine and dioxidation events on tryptophan. A few proteins are exquisitely sensitive to targeted oxidation events, notably the active site of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in <i>E. coli</i>. Extensive experimental evolution of <i>E. coli</i> for IR resistance has decreased overall proteome sensitivity to oxidation but not to the level seen in <i>D. radiodurans</i>. Many observed oxidation events may reflect aspects of protein structure and/or exposure of protein surfaces to water. Proteins such as GAPDH and possibly Ef-Tu may have an evolved sensitivity to oxidation by H<sub>2</sub>O<sub>2</sub>.
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spelling doaj.art-a4f24d79d15d43488a7e3931f73acc612023-11-21T16:20:04ZengMDPI AGCells2073-44092021-04-0110495410.3390/cells10040954Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav RadmanSteven T. Bruckbauer0Benjamin B. Minkoff1Michael R. Sussman2Michael M. Cox3Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USACenter for Genomic Science Innovation, University of Wisconsin-Madison, Madison, WI 53706, USADepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USADepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USAOxidative proteome damage has been implicated as a major contributor to cell death and aging. Protein damage and aging has been a particular theme of the recent research of Miroslav Radman. However, the study of how cellular proteins are damaged by oxidative processes is still in its infancy. Here we examine oxidative changes in the proteomes of four bacterial populations—wild type <i>E. coli</i>, two isolates from <i>E. coli</i> populations evolved for high levels of ionizing radiation (IR) resistance, and <i>D. radiodurans</i>—immediately following exposure to 3000 Gy of ionizing radiation. By a substantial margin, the most prominent intracellular oxidation events involve hydroxylation of methionine residues. Significant but much less frequent are carbonylation events on tyrosine and dioxidation events on tryptophan. A few proteins are exquisitely sensitive to targeted oxidation events, notably the active site of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in <i>E. coli</i>. Extensive experimental evolution of <i>E. coli</i> for IR resistance has decreased overall proteome sensitivity to oxidation but not to the level seen in <i>D. radiodurans</i>. Many observed oxidation events may reflect aspects of protein structure and/or exposure of protein surfaces to water. Proteins such as GAPDH and possibly Ef-Tu may have an evolved sensitivity to oxidation by H<sub>2</sub>O<sub>2</sub>.https://www.mdpi.com/2073-4409/10/4/954proteome<i>Escherichia coli</i><i>Deinococcus radiodurans</i>reactive oxygen speciesprotein damageionizing radiation
spellingShingle Steven T. Bruckbauer
Benjamin B. Minkoff
Michael R. Sussman
Michael M. Cox
Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
Cells
proteome
<i>Escherichia coli</i>
<i>Deinococcus radiodurans</i>
reactive oxygen species
protein damage
ionizing radiation
title Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
title_full Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
title_fullStr Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
title_full_unstemmed Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
title_short Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman
title_sort proteome damage inflicted by ionizing radiation advancing a theme in the research of miroslav radman
topic proteome
<i>Escherichia coli</i>
<i>Deinococcus radiodurans</i>
reactive oxygen species
protein damage
ionizing radiation
url https://www.mdpi.com/2073-4409/10/4/954
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