Differential roles of the hemerythrin-like proteins of Mycobacterium smegmatis in hydrogen peroxide and erythromycin susceptibility
Hemerythrin-like proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on oxidation-reduction regulation and antibiotic resistance. Recent studies using bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have been acq...
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| Veröffentlicht in: | Scientific reports 2015-11, Vol.5 (1), p.16130-16130, Article 16130 |
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| creator | Li, Xiaojing Li, Jingjing Hu, Xinling Huang, Lige Xiao, Jing Chan, John Mi, Kaixia |
| description | Hemerythrin-like proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on oxidation-reduction regulation and antibiotic resistance. Recent studies using bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have been acquired by lateral gene transfer and the number of hemerythrin-like proteins varies amongst different species.
Mycobacterium smegmatis
contains three hemerythrin-like proteins, MSMEG_3312, MSMEG_2415 and MSMEG_6212. In this study, we have systematically analyzed all three hemerythrin-like proteins in
M. smegmatis
and our results identified and characterized two functional classes: MSMEG_2415 plays an important role in H
2
O
2
susceptibility and MSMEG_3312 and MSMEG_6212 are associated with erythromycin susceptibility. Phylogenetic analysis indicated that these three proteins have different evolutionary origins, possibly explaining their different physiological functions. Here, combined with biological and phylogenetic analyses, our results provide new insights into the evolutionary divergence of the hemerythrin-like proteins in
M. smegmatis. |
| doi_str_mv | 10.1038/srep16130 |
| format | Article |
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Mycobacterium smegmatis
contains three hemerythrin-like proteins, MSMEG_3312, MSMEG_2415 and MSMEG_6212. In this study, we have systematically analyzed all three hemerythrin-like proteins in
M. smegmatis
and our results identified and characterized two functional classes: MSMEG_2415 plays an important role in H
2
O
2
susceptibility and MSMEG_3312 and MSMEG_6212 are associated with erythromycin susceptibility. Phylogenetic analysis indicated that these three proteins have different evolutionary origins, possibly explaining their different physiological functions. Here, combined with biological and phylogenetic analyses, our results provide new insights into the evolutionary divergence of the hemerythrin-like proteins in
M. smegmatis.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep16130</identifier><identifier>PMID: 26607739</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/326/1320 ; 631/326/41/2482 ; Adaptation, Physiological - drug effects ; Bacterial Proteins - metabolism ; Erythromycin - pharmacology ; Gene Knockout Techniques ; Hemerythrin - metabolism ; Humanities and Social Sciences ; Hydrogen Peroxide - pharmacology ; Microbial Sensitivity Tests ; Models, Biological ; multidisciplinary ; Mycobacterium smegmatis - drug effects ; Mycobacterium smegmatis - metabolism ; Phylogeny ; Science</subject><ispartof>Scientific reports, 2015-11, Vol.5 (1), p.16130-16130, Article 16130</ispartof><rights>The Author(s) 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c410t-7df1f2c5bd7b6ee9b5b326ea1a22d7a9e8e85f6ddca99556f706bc4f29d268bd3</citedby><cites>FETCH-LOGICAL-c410t-7df1f2c5bd7b6ee9b5b326ea1a22d7a9e8e85f6ddca99556f706bc4f29d268bd3</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/PMC4660385/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660385/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26607739$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Xiaojing</creatorcontrib><creatorcontrib>Li, Jingjing</creatorcontrib><creatorcontrib>Hu, Xinling</creatorcontrib><creatorcontrib>Huang, Lige</creatorcontrib><creatorcontrib>Xiao, Jing</creatorcontrib><creatorcontrib>Chan, John</creatorcontrib><creatorcontrib>Mi, Kaixia</creatorcontrib><title>Differential roles of the hemerythrin-like proteins of Mycobacterium smegmatis in hydrogen peroxide and erythromycin susceptibility</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Hemerythrin-like proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on oxidation-reduction regulation and antibiotic resistance. Recent studies using bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have been acquired by lateral gene transfer and the number of hemerythrin-like proteins varies amongst different species.
Mycobacterium smegmatis
contains three hemerythrin-like proteins, MSMEG_3312, MSMEG_2415 and MSMEG_6212. In this study, we have systematically analyzed all three hemerythrin-like proteins in
M. smegmatis
and our results identified and characterized two functional classes: MSMEG_2415 plays an important role in H
2
O
2
susceptibility and MSMEG_3312 and MSMEG_6212 are associated with erythromycin susceptibility. Phylogenetic analysis indicated that these three proteins have different evolutionary origins, possibly explaining their different physiological functions. Here, combined with biological and phylogenetic analyses, our results provide new insights into the evolutionary divergence of the hemerythrin-like proteins in
M. smegmatis.</description><subject>631/326/1320</subject><subject>631/326/41/2482</subject><subject>Adaptation, Physiological - drug effects</subject><subject>Bacterial Proteins - metabolism</subject><subject>Erythromycin - pharmacology</subject><subject>Gene Knockout Techniques</subject><subject>Hemerythrin - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Microbial Sensitivity Tests</subject><subject>Models, Biological</subject><subject>multidisciplinary</subject><subject>Mycobacterium smegmatis - drug effects</subject><subject>Mycobacterium smegmatis - metabolism</subject><subject>Phylogeny</subject><subject>Science</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><recordid>eNptkc1u1TAQRi0EolXpghdAXgJSwD-Jk2yQUKFQqVU3sLYce3zjktjBdhBZ98XrcstVkfDGluboeGY-hF5S8o4S3r1PERYqKCdP0DEjdVMxztjTR-8jdJrSDSmnYX1N--foiAlB2pb3x-j2k7MWIvjs1IRjmCDhYHEeAY8wQ9zyGJ2vJvcD8BJDBuf_AFebDoPSGaJbZ5xm2M0qu4Sdx-NmYtiBxwvE8NsZwMobvFeFedMFSWvSsGQ3uMnl7QV6ZtWU4PThPkHfzz9_O_taXV5_uTj7eFnpmpJctcZSy3QzmHYQAP3QDJwJUFQxZlrVQwddY4UxWvV90wjbEjHo2rLeMNENhp-gD3vvsg4zGF2GjmqSS3SzipsMysl_K96Nchd-ybqsi3dNEbx-EMTwc4WU5ezKINOkPIQ1Sdryru4ob-_RN3tUx5BKRPbwDSXyPjd5yK2wrx73dSD_plSAt3sglZLfQZQ3YY2-7Oo_tjsq3KgA</recordid><startdate>20151126</startdate><enddate>20151126</enddate><creator>Li, Xiaojing</creator><creator>Li, Jingjing</creator><creator>Hu, Xinling</creator><creator>Huang, Lige</creator><creator>Xiao, Jing</creator><creator>Chan, John</creator><creator>Mi, Kaixia</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20151126</creationdate><title>Differential roles of the hemerythrin-like proteins of Mycobacterium smegmatis in hydrogen peroxide and erythromycin susceptibility</title><author>Li, Xiaojing ; Li, Jingjing ; Hu, Xinling ; Huang, Lige ; Xiao, Jing ; Chan, John ; Mi, Kaixia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c410t-7df1f2c5bd7b6ee9b5b326ea1a22d7a9e8e85f6ddca99556f706bc4f29d268bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>631/326/1320</topic><topic>631/326/41/2482</topic><topic>Adaptation, Physiological - drug effects</topic><topic>Bacterial Proteins - metabolism</topic><topic>Erythromycin - pharmacology</topic><topic>Gene Knockout Techniques</topic><topic>Hemerythrin - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Microbial Sensitivity Tests</topic><topic>Models, Biological</topic><topic>multidisciplinary</topic><topic>Mycobacterium smegmatis - drug effects</topic><topic>Mycobacterium smegmatis - metabolism</topic><topic>Phylogeny</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Xiaojing</creatorcontrib><creatorcontrib>Li, Jingjing</creatorcontrib><creatorcontrib>Hu, Xinling</creatorcontrib><creatorcontrib>Huang, Lige</creatorcontrib><creatorcontrib>Xiao, Jing</creatorcontrib><creatorcontrib>Chan, John</creatorcontrib><creatorcontrib>Mi, Kaixia</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Xiaojing</au><au>Li, Jingjing</au><au>Hu, Xinling</au><au>Huang, Lige</au><au>Xiao, Jing</au><au>Chan, John</au><au>Mi, Kaixia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential roles of the hemerythrin-like proteins of Mycobacterium smegmatis in hydrogen peroxide and erythromycin susceptibility</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-11-26</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>16130</spage><epage>16130</epage><pages>16130-16130</pages><artnum>16130</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Hemerythrin-like proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on oxidation-reduction regulation and antibiotic resistance. Recent studies using bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have been acquired by lateral gene transfer and the number of hemerythrin-like proteins varies amongst different species.
Mycobacterium smegmatis
contains three hemerythrin-like proteins, MSMEG_3312, MSMEG_2415 and MSMEG_6212. In this study, we have systematically analyzed all three hemerythrin-like proteins in
M. smegmatis
and our results identified and characterized two functional classes: MSMEG_2415 plays an important role in H
2
O
2
susceptibility and MSMEG_3312 and MSMEG_6212 are associated with erythromycin susceptibility. Phylogenetic analysis indicated that these three proteins have different evolutionary origins, possibly explaining their different physiological functions. Here, combined with biological and phylogenetic analyses, our results provide new insights into the evolutionary divergence of the hemerythrin-like proteins in
M. smegmatis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26607739</pmid><doi>10.1038/srep16130</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Springer Nature OA Free Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 631/326/1320 631/326/41/2482 Adaptation, Physiological - drug effects Bacterial Proteins - metabolism Erythromycin - pharmacology Gene Knockout Techniques Hemerythrin - metabolism Humanities and Social Sciences Hydrogen Peroxide - pharmacology Microbial Sensitivity Tests Models, Biological multidisciplinary Mycobacterium smegmatis - drug effects Mycobacterium smegmatis - metabolism Phylogeny Science |
| title | Differential roles of the hemerythrin-like proteins of Mycobacterium smegmatis in hydrogen peroxide and erythromycin susceptibility |
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