A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction
Iron is an essential metal for living organisms but its level must be strictly controlled in cells, because ferrous ion induces toxicity by generating highly active reactive oxygen, hydroxyl radicals, through the Fenton reaction. In addition, ferric ion shows low solubility under physiological condi...
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| Veröffentlicht in: | PloS one 2011-06, Vol.6 (6), p.e20985-e20985 |
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| creator | Takatsuka, Masaki Osada-Oka, Mayuko Satoh, Eisuke F Kitadokoro, Kengo Nishiuchi, Yukiko Niki, Mamiko Inoue, Masayasu Iwai, Kazuhiro Arakawa, Tetsuo Shimoji, Yoshihiro Ogura, Hisashi Kobayashi, Kazuo Rambukkana, Anura Matsumoto, Sohkichi |
| description | Iron is an essential metal for living organisms but its level must be strictly controlled in cells, because ferrous ion induces toxicity by generating highly active reactive oxygen, hydroxyl radicals, through the Fenton reaction. In addition, ferric ion shows low solubility under physiological conditions. To overcome these obstacles living organisms possess Ferritin superfamily proteins that are distributed in all three domains of life: bacteria, archaea, and eukaryotes. These proteins minimize hydroxyl radical formation by ferroxidase activity that converts Fe(2+) into Fe(3+) and sequesters iron by storing it as a mineral inside a protein cage. In this study, we discovered that mycobacterial DNA-binding protein 1 (MDP1), a histone-like protein, has similar activity to ferritin superfamily proteins. MDP1 prevented the Fenton reaction and protects DNA by the ferroxidase activity. The K(m) values of the ferroxidase activity by MDP1 of Mycobacterium bovis bacillus Calmette-Guérin (BCG-3007c), Mycobacterium tuberculosis (Rv2986c), and Mycobacterium leprae (ML1683; ML-LBP) were 0.292, 0.252, and 0.129 mM, respectively. Furthermore, one MDP1 molecule directly captured 81.4±19.1 iron atoms, suggesting the role of this protein in iron storage. This study describes for the first time a ferroxidase-iron storage protein outside of the ferritin superfamily proteins and the protective role of this bacterial protein from DNA damage. |
| doi_str_mv | 10.1371/journal.pone.0020985 |
| format | Article |
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In addition, ferric ion shows low solubility under physiological conditions. To overcome these obstacles living organisms possess Ferritin superfamily proteins that are distributed in all three domains of life: bacteria, archaea, and eukaryotes. These proteins minimize hydroxyl radical formation by ferroxidase activity that converts Fe(2+) into Fe(3+) and sequesters iron by storing it as a mineral inside a protein cage. In this study, we discovered that mycobacterial DNA-binding protein 1 (MDP1), a histone-like protein, has similar activity to ferritin superfamily proteins. MDP1 prevented the Fenton reaction and protects DNA by the ferroxidase activity. The K(m) values of the ferroxidase activity by MDP1 of Mycobacterium bovis bacillus Calmette-Guérin (BCG-3007c), Mycobacterium tuberculosis (Rv2986c), and Mycobacterium leprae (ML1683; ML-LBP) were 0.292, 0.252, and 0.129 mM, respectively. Furthermore, one MDP1 molecule directly captured 81.4±19.1 iron atoms, suggesting the role of this protein in iron storage. This study describes for the first time a ferroxidase-iron storage protein outside of the ferritin superfamily proteins and the protective role of this bacterial protein from DNA damage.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0020985</identifier><identifier>PMID: 21698192</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Active control ; Antigens ; Archaea ; Bacillus Calmette-Guerin vaccine ; Bacteria ; Bacteriology ; BCG ; Biology ; Ceruloplasmin - metabolism ; Deoxyribonucleic acid ; DNA ; DNA Damage ; DNA-binding protein ; Enzyme kinetics ; Eukaryotes ; Ferritin ; Ferritins - physiology ; Ferroxidase ; Free radicals ; Gastroenterology ; Histones - physiology ; Homeostasis ; Hydroxides ; Hydroxyl radical formation ; Hydroxyl radicals ; Infectious diseases ; Iron ; Leprosy ; Medicine ; Mycobacterium - enzymology ; Mycobacterium - metabolism ; Mycobacterium avium ; Mycobacterium leprae ; Mycobacterium smegmatis ; Mycobacterium tuberculosis ; Oxygen ; Phylogeny ; Physiological aspects ; Physiology ; Protein Binding ; Proteins ; Solubility ; Storage ; Toxicity ; Tuberculosis ; University graduates</subject><ispartof>PloS one, 2011-06, Vol.6 (6), p.e20985-e20985</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Takatsuka et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Takatsuka et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c757t-9745c0ccdaf43cff18760a64a7a67ba34b7215b653ff89dcc80bb4c843e322503</citedby><cites>FETCH-LOGICAL-c757t-9745c0ccdaf43cff18760a64a7a67ba34b7215b653ff89dcc80bb4c843e322503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3116847/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3116847/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79472,79473</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21698192$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bereswill, Stefan</contributor><creatorcontrib>Takatsuka, Masaki</creatorcontrib><creatorcontrib>Osada-Oka, Mayuko</creatorcontrib><creatorcontrib>Satoh, Eisuke F</creatorcontrib><creatorcontrib>Kitadokoro, Kengo</creatorcontrib><creatorcontrib>Nishiuchi, Yukiko</creatorcontrib><creatorcontrib>Niki, Mamiko</creatorcontrib><creatorcontrib>Inoue, Masayasu</creatorcontrib><creatorcontrib>Iwai, Kazuhiro</creatorcontrib><creatorcontrib>Arakawa, Tetsuo</creatorcontrib><creatorcontrib>Shimoji, Yoshihiro</creatorcontrib><creatorcontrib>Ogura, Hisashi</creatorcontrib><creatorcontrib>Kobayashi, Kazuo</creatorcontrib><creatorcontrib>Rambukkana, Anura</creatorcontrib><creatorcontrib>Matsumoto, Sohkichi</creatorcontrib><title>A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Iron is an essential metal for living organisms but its level must be strictly controlled in cells, because ferrous ion induces toxicity by generating highly active reactive oxygen, hydroxyl radicals, through the Fenton reaction. In addition, ferric ion shows low solubility under physiological conditions. To overcome these obstacles living organisms possess Ferritin superfamily proteins that are distributed in all three domains of life: bacteria, archaea, and eukaryotes. These proteins minimize hydroxyl radical formation by ferroxidase activity that converts Fe(2+) into Fe(3+) and sequesters iron by storing it as a mineral inside a protein cage. In this study, we discovered that mycobacterial DNA-binding protein 1 (MDP1), a histone-like protein, has similar activity to ferritin superfamily proteins. MDP1 prevented the Fenton reaction and protects DNA by the ferroxidase activity. The K(m) values of the ferroxidase activity by MDP1 of Mycobacterium bovis bacillus Calmette-Guérin (BCG-3007c), Mycobacterium tuberculosis (Rv2986c), and Mycobacterium leprae (ML1683; ML-LBP) were 0.292, 0.252, and 0.129 mM, respectively. Furthermore, one MDP1 molecule directly captured 81.4±19.1 iron atoms, suggesting the role of this protein in iron storage. This study describes for the first time a ferroxidase-iron storage protein outside of the ferritin superfamily proteins and the protective role of this bacterial protein from DNA damage.</description><subject>Active control</subject><subject>Antigens</subject><subject>Archaea</subject><subject>Bacillus Calmette-Guerin vaccine</subject><subject>Bacteria</subject><subject>Bacteriology</subject><subject>BCG</subject><subject>Biology</subject><subject>Ceruloplasmin - metabolism</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Damage</subject><subject>DNA-binding protein</subject><subject>Enzyme kinetics</subject><subject>Eukaryotes</subject><subject>Ferritin</subject><subject>Ferritins - physiology</subject><subject>Ferroxidase</subject><subject>Free radicals</subject><subject>Gastroenterology</subject><subject>Histones - physiology</subject><subject>Homeostasis</subject><subject>Hydroxides</subject><subject>Hydroxyl radical formation</subject><subject>Hydroxyl radicals</subject><subject>Infectious diseases</subject><subject>Iron</subject><subject>Leprosy</subject><subject>Medicine</subject><subject>Mycobacterium - enzymology</subject><subject>Mycobacterium - metabolism</subject><subject>Mycobacterium avium</subject><subject>Mycobacterium leprae</subject><subject>Mycobacterium smegmatis</subject><subject>Mycobacterium tuberculosis</subject><subject>Oxygen</subject><subject>Phylogeny</subject><subject>Physiological aspects</subject><subject>Physiology</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Solubility</subject><subject>Storage</subject><subject>Toxicity</subject><subject>Tuberculosis</subject><subject>University graduates</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk9-K1DAUxoso7rr6BqIBQfFixqRJk_RGGFZXBxYX_Hcb0jSZydo2NUkX5yV8ZlOns0xlL6SFhuT3fefk9Jwse4rgEmGG3ly7wXeyWfau00sIc1jy4l52ikqcL2gO8f2j9Un2KIRrCAvMKX2YneSIlhyV-Wn2ewW2NsTksWjsDw1676K2HXAGtDvlKqmi9laC3oWgxxcY7b2NCQlDr72RrW12B9neI2nsjY07ILt6f6JiAHIjbRciePdpBWrZyo0G1Q5c6C4FB16PItc9zh4Y2QT9ZPqeZd8u3n89_7i4vPqwPl9dLhQrWFyUjBQKKlVLQ7AyBnFGoaREMklZJTGpWI6KihbYGF7WSnFYVURxgjXO8wLis-z53rdvXBBTKYNAGBLGICUkEes9UTt5LXpvW-l3wkkr_m44vxHSR6saLVipCEEVSxUtScqohJBWCjJVs5QSVsnr7RRtqFpdq3RnL5uZ6fyks1uxcTcCI0Q5Ycng1WTg3c9BhyhaG5RuGtlpNwTBGWawQAVN5It_yLsvN1EbmfK3nXEprBo9xYowyjnjtEzU8g4qPbVurUotY2zanwlezwSJifpX3MghBLH-8vn_2avvc_blEbvVsonb4Jph7JgwB8keVD71q9fmtsYIinFqDtUQ49SIaWqS7Nnx_7kVHcYE_wHHXhTd</recordid><startdate>20110616</startdate><enddate>20110616</enddate><creator>Takatsuka, Masaki</creator><creator>Osada-Oka, Mayuko</creator><creator>Satoh, Eisuke F</creator><creator>Kitadokoro, Kengo</creator><creator>Nishiuchi, Yukiko</creator><creator>Niki, Mamiko</creator><creator>Inoue, Masayasu</creator><creator>Iwai, Kazuhiro</creator><creator>Arakawa, Tetsuo</creator><creator>Shimoji, Yoshihiro</creator><creator>Ogura, Hisashi</creator><creator>Kobayashi, Kazuo</creator><creator>Rambukkana, Anura</creator><creator>Matsumoto, Sohkichi</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110616</creationdate><title>A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction</title><author>Takatsuka, Masaki ; Osada-Oka, Mayuko ; Satoh, Eisuke F ; Kitadokoro, Kengo ; Nishiuchi, Yukiko ; Niki, Mamiko ; Inoue, Masayasu ; Iwai, Kazuhiro ; Arakawa, Tetsuo ; Shimoji, Yoshihiro ; Ogura, Hisashi ; Kobayashi, Kazuo ; Rambukkana, Anura ; Matsumoto, Sohkichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c757t-9745c0ccdaf43cff18760a64a7a67ba34b7215b653ff89dcc80bb4c843e322503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Active control</topic><topic>Antigens</topic><topic>Archaea</topic><topic>Bacillus Calmette-Guerin vaccine</topic><topic>Bacteria</topic><topic>Bacteriology</topic><topic>BCG</topic><topic>Biology</topic><topic>Ceruloplasmin - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takatsuka, Masaki</au><au>Osada-Oka, Mayuko</au><au>Satoh, Eisuke F</au><au>Kitadokoro, Kengo</au><au>Nishiuchi, Yukiko</au><au>Niki, Mamiko</au><au>Inoue, Masayasu</au><au>Iwai, Kazuhiro</au><au>Arakawa, Tetsuo</au><au>Shimoji, Yoshihiro</au><au>Ogura, Hisashi</au><au>Kobayashi, Kazuo</au><au>Rambukkana, Anura</au><au>Matsumoto, Sohkichi</au><au>Bereswill, Stefan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-06-16</date><risdate>2011</risdate><volume>6</volume><issue>6</issue><spage>e20985</spage><epage>e20985</epage><pages>e20985-e20985</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Iron is an essential metal for living organisms but its level must be strictly controlled in cells, because ferrous ion induces toxicity by generating highly active reactive oxygen, hydroxyl radicals, through the Fenton reaction. In addition, ferric ion shows low solubility under physiological conditions. To overcome these obstacles living organisms possess Ferritin superfamily proteins that are distributed in all three domains of life: bacteria, archaea, and eukaryotes. These proteins minimize hydroxyl radical formation by ferroxidase activity that converts Fe(2+) into Fe(3+) and sequesters iron by storing it as a mineral inside a protein cage. In this study, we discovered that mycobacterial DNA-binding protein 1 (MDP1), a histone-like protein, has similar activity to ferritin superfamily proteins. MDP1 prevented the Fenton reaction and protects DNA by the ferroxidase activity. The K(m) values of the ferroxidase activity by MDP1 of Mycobacterium bovis bacillus Calmette-Guérin (BCG-3007c), Mycobacterium tuberculosis (Rv2986c), and Mycobacterium leprae (ML1683; ML-LBP) were 0.292, 0.252, and 0.129 mM, respectively. Furthermore, one MDP1 molecule directly captured 81.4±19.1 iron atoms, suggesting the role of this protein in iron storage. This study describes for the first time a ferroxidase-iron storage protein outside of the ferritin superfamily proteins and the protective role of this bacterial protein from DNA damage.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21698192</pmid><doi>10.1371/journal.pone.0020985</doi><tpages>e20985</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2011-06, Vol.6 (6), p.e20985-e20985 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1304770644 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Active control Antigens Archaea Bacillus Calmette-Guerin vaccine Bacteria Bacteriology BCG Biology Ceruloplasmin - metabolism Deoxyribonucleic acid DNA DNA Damage DNA-binding protein Enzyme kinetics Eukaryotes Ferritin Ferritins - physiology Ferroxidase Free radicals Gastroenterology Histones - physiology Homeostasis Hydroxides Hydroxyl radical formation Hydroxyl radicals Infectious diseases Iron Leprosy Medicine Mycobacterium - enzymology Mycobacterium - metabolism Mycobacterium avium Mycobacterium leprae Mycobacterium smegmatis Mycobacterium tuberculosis Oxygen Phylogeny Physiological aspects Physiology Protein Binding Proteins Solubility Storage Toxicity Tuberculosis University graduates |
| title | A histone-like protein of mycobacteria possesses ferritin superfamily protein-like activity and protects against DNA damage by Fenton reaction |
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