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Oxidant-Mediated Protein Amino Acid Conversion
Biological oxidation plays important roles in the pathogenesis of various diseases and aging. Carbonylation is one mode of protein oxidation. It has been reported that amino acids that are susceptible to carbonylation are arginine (Arg), proline (Pro), lysine, and threonine residues. The carbonylati...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6406366/ https://www.ncbi.nlm.nih.gov/pubmed/30823521 http://dx.doi.org/10.3390/antiox8020050 |
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author | Suzuki, Yuichiro J. |
author_facet | Suzuki, Yuichiro J. |
author_sort | Suzuki, Yuichiro J. |
collection | PubMed |
description | Biological oxidation plays important roles in the pathogenesis of various diseases and aging. Carbonylation is one mode of protein oxidation. It has been reported that amino acids that are susceptible to carbonylation are arginine (Arg), proline (Pro), lysine, and threonine residues. The carbonylation product of both Arg and Pro residues is glutamyl semialdehyde. While chemically the oxidation reactions of neither Pro to glutamyl semialdehyde nor Arg to glutamyl semialdehyde are reversible, experimental results from our laboratory suggest that the biological system may drive the reduction of glutamyl semialdehyde to Pro in the protein structure. Further, glutamyl semialdehyde can be oxidized to become glutamic acid (Glu). Therefore, I hypothesize that biological oxidation post-translationally converts Arg to Pro, Arg to Glu, and Pro to Glu within the protein structure. Our mass spectrometry experiments provided evidence that, in human cells, 5–10% of peroxiredoxin 6 protein molecules have Pro-45 replaced by Glu. This concept of protein amino acid conversion challenges the dogma that amino acid sequences are strictly defined by nucleic acid sequences. I propose that, in the biological system, amino acid replacements can occur post-translationally through redox regulation, and protein molecules with non-DNA coding sequences confer functions. |
format | Online Article Text |
id | pubmed-6406366 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-64063662019-03-08 Oxidant-Mediated Protein Amino Acid Conversion Suzuki, Yuichiro J. Antioxidants (Basel) Review Biological oxidation plays important roles in the pathogenesis of various diseases and aging. Carbonylation is one mode of protein oxidation. It has been reported that amino acids that are susceptible to carbonylation are arginine (Arg), proline (Pro), lysine, and threonine residues. The carbonylation product of both Arg and Pro residues is glutamyl semialdehyde. While chemically the oxidation reactions of neither Pro to glutamyl semialdehyde nor Arg to glutamyl semialdehyde are reversible, experimental results from our laboratory suggest that the biological system may drive the reduction of glutamyl semialdehyde to Pro in the protein structure. Further, glutamyl semialdehyde can be oxidized to become glutamic acid (Glu). Therefore, I hypothesize that biological oxidation post-translationally converts Arg to Pro, Arg to Glu, and Pro to Glu within the protein structure. Our mass spectrometry experiments provided evidence that, in human cells, 5–10% of peroxiredoxin 6 protein molecules have Pro-45 replaced by Glu. This concept of protein amino acid conversion challenges the dogma that amino acid sequences are strictly defined by nucleic acid sequences. I propose that, in the biological system, amino acid replacements can occur post-translationally through redox regulation, and protein molecules with non-DNA coding sequences confer functions. MDPI 2019-02-25 /pmc/articles/PMC6406366/ /pubmed/30823521 http://dx.doi.org/10.3390/antiox8020050 Text en © 2019 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Suzuki, Yuichiro J. Oxidant-Mediated Protein Amino Acid Conversion |
title | Oxidant-Mediated Protein Amino Acid Conversion |
title_full | Oxidant-Mediated Protein Amino Acid Conversion |
title_fullStr | Oxidant-Mediated Protein Amino Acid Conversion |
title_full_unstemmed | Oxidant-Mediated Protein Amino Acid Conversion |
title_short | Oxidant-Mediated Protein Amino Acid Conversion |
title_sort | oxidant-mediated protein amino acid conversion |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6406366/ https://www.ncbi.nlm.nih.gov/pubmed/30823521 http://dx.doi.org/10.3390/antiox8020050 |
work_keys_str_mv | AT suzukiyuichiroj oxidantmediatedproteinaminoacidconversion |