Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp
Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focuse...
Gespeichert in:
Veröffentlicht in: | Free radical biology & medicine 2011, Vol.50 (1), p.37-46 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 46 |
---|---|
container_issue | 1 |
container_start_page | 37 |
container_title | Free radical biology & medicine |
container_volume | 50 |
creator | Arias, Diego G. Cabeza, Matías S. Erben, Esteban D. Carranza, Pedro G. Lujan, Hugo D. Téllez Iñón, María T. Iglesias, Alberto A. Guerrero, Sergio A. |
description | Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in
Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(
S)SO reduction, using
Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of
T. cruzi and
Trypanosoma brucei. The results support the occurrence of a metabolic pathway in
Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules. |
doi_str_mv | 10.1016/j.freeradbiomed.2010.10.695 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_822363776</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0891584910013183</els_id><sourcerecordid>822363776</sourcerecordid><originalsourceid>FETCH-LOGICAL-c459t-49dadd549afb7355e66b7dad0f175f919371f6d2a9d7ca3e852be37f1f744ae13</originalsourceid><addsrcrecordid>eNqNkMFu1DAQhi0EokvhFSASB05Z7Di2Y3GqqhaQKnFge7Ym9ph6lcTBTirK0-Ow7YEbJ1sz38z8-gh5z-ieUSY_Hvc-ISZwfYgjun1D_3b2UotnZMc6xetWaPmc7GinWS26Vp-RVzkfKaWt4N1LctZQLbUWzY4crtfJLiFOMFT2DhLYBVP4DVupir4acbkr3zBhldfBx1_BYZXQrXaBjNVF5VMcq0N6mGGKOY5Q5Xl-TV54GDK-eXzPye311eHyS33z7fPXy4ub2paAS91qB86JVoPvFRcCpexVKVHPlPCaaa6Yl64B7ZQFjp1oeuTKM6_aFpDxc_LhtHdO8eeKeTFjyBaHASaMazZd03DJlZKF_HQibYo5J_RmTmGE9GAYNZtVczT_WDWb1a1ZrJbpt4931n7rPc0-aSzAuxPgIRr4kUI2t9_LBkEpKwkaXoirE4HFx33AZLINOFl0IaFdjIvhv6L8ASVQm7w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>822363776</pqid></control><display><type>article</type><title>Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Arias, Diego G. ; Cabeza, Matías S. ; Erben, Esteban D. ; Carranza, Pedro G. ; Lujan, Hugo D. ; Téllez Iñón, María T. ; Iglesias, Alberto A. ; Guerrero, Sergio A.</creator><creatorcontrib>Arias, Diego G. ; Cabeza, Matías S. ; Erben, Esteban D. ; Carranza, Pedro G. ; Lujan, Hugo D. ; Téllez Iñón, María T. ; Iglesias, Alberto A. ; Guerrero, Sergio A.</creatorcontrib><description>Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in
Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(
S)SO reduction, using
Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of
T. cruzi and
Trypanosoma brucei. The results support the occurrence of a metabolic pathway in
Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules.</description><identifier>ISSN: 0891-5849</identifier><identifier>EISSN: 1873-4596</identifier><identifier>DOI: 10.1016/j.freeradbiomed.2010.10.695</identifier><identifier>PMID: 20969952</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; antioxidants ; biochemical pathways ; Cells, Cultured ; Cercopithecus aethiops ; Cloning, Molecular ; developmental stages ; electrophoresis ; enzymes ; Escherichia coli ; Free radicals ; gene expression ; genes ; Metabolic Detoxication, Phase I - genetics ; Metabolic Networks and Pathways - genetics ; methionine ; Methionine sulfoxide ; Methionine Sulfoxide Reductases - chemistry ; Methionine Sulfoxide Reductases - genetics ; Methionine Sulfoxide Reductases - isolation & purification ; Methionine Sulfoxide Reductases - metabolism ; Models, Molecular ; molecular cloning ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidative stress ; Oxidative Stress - genetics ; pathogens ; recombinant proteins ; Sequence Homology ; Trypanosoma ; Trypanosoma - enzymology ; Trypanosoma - genetics ; Trypanosoma brucei ; Trypanosoma brucei brucei - enzymology ; Trypanosoma brucei brucei - genetics ; Trypanosoma brucei brucei - metabolism ; Trypanosoma cruzi ; Trypanosoma cruzi - enzymology ; Trypanosoma cruzi - genetics ; Trypanosoma cruzi - metabolism ; Trypanothione ; Tryparedoxin ; Vero Cells</subject><ispartof>Free radical biology & medicine, 2011, Vol.50 (1), p.37-46</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright © 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-49dadd549afb7355e66b7dad0f175f919371f6d2a9d7ca3e852be37f1f744ae13</citedby><cites>FETCH-LOGICAL-c459t-49dadd549afb7355e66b7dad0f175f919371f6d2a9d7ca3e852be37f1f744ae13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.freeradbiomed.2010.10.695$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,4010,27904,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20969952$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arias, Diego G.</creatorcontrib><creatorcontrib>Cabeza, Matías S.</creatorcontrib><creatorcontrib>Erben, Esteban D.</creatorcontrib><creatorcontrib>Carranza, Pedro G.</creatorcontrib><creatorcontrib>Lujan, Hugo D.</creatorcontrib><creatorcontrib>Téllez Iñón, María T.</creatorcontrib><creatorcontrib>Iglesias, Alberto A.</creatorcontrib><creatorcontrib>Guerrero, Sergio A.</creatorcontrib><title>Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp</title><title>Free radical biology & medicine</title><addtitle>Free Radic Biol Med</addtitle><description>Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in
Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(
S)SO reduction, using
Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of
T. cruzi and
Trypanosoma brucei. The results support the occurrence of a metabolic pathway in
Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>antioxidants</subject><subject>biochemical pathways</subject><subject>Cells, Cultured</subject><subject>Cercopithecus aethiops</subject><subject>Cloning, Molecular</subject><subject>developmental stages</subject><subject>electrophoresis</subject><subject>enzymes</subject><subject>Escherichia coli</subject><subject>Free radicals</subject><subject>gene expression</subject><subject>genes</subject><subject>Metabolic Detoxication, Phase I - genetics</subject><subject>Metabolic Networks and Pathways - genetics</subject><subject>methionine</subject><subject>Methionine sulfoxide</subject><subject>Methionine Sulfoxide Reductases - chemistry</subject><subject>Methionine Sulfoxide Reductases - genetics</subject><subject>Methionine Sulfoxide Reductases - isolation & purification</subject><subject>Methionine Sulfoxide Reductases - metabolism</subject><subject>Models, Molecular</subject><subject>molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>Oxidation-Reduction</subject><subject>Oxidative stress</subject><subject>Oxidative Stress - genetics</subject><subject>pathogens</subject><subject>recombinant proteins</subject><subject>Sequence Homology</subject><subject>Trypanosoma</subject><subject>Trypanosoma - enzymology</subject><subject>Trypanosoma - genetics</subject><subject>Trypanosoma brucei</subject><subject>Trypanosoma brucei brucei - enzymology</subject><subject>Trypanosoma brucei brucei - genetics</subject><subject>Trypanosoma brucei brucei - metabolism</subject><subject>Trypanosoma cruzi</subject><subject>Trypanosoma cruzi - enzymology</subject><subject>Trypanosoma cruzi - genetics</subject><subject>Trypanosoma cruzi - metabolism</subject><subject>Trypanothione</subject><subject>Tryparedoxin</subject><subject>Vero Cells</subject><issn>0891-5849</issn><issn>1873-4596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMFu1DAQhi0EokvhFSASB05Z7Di2Y3GqqhaQKnFge7Ym9ph6lcTBTirK0-Ow7YEbJ1sz38z8-gh5z-ieUSY_Hvc-ISZwfYgjun1D_3b2UotnZMc6xetWaPmc7GinWS26Vp-RVzkfKaWt4N1LctZQLbUWzY4crtfJLiFOMFT2DhLYBVP4DVupir4acbkr3zBhldfBx1_BYZXQrXaBjNVF5VMcq0N6mGGKOY5Q5Xl-TV54GDK-eXzPye311eHyS33z7fPXy4ub2paAS91qB86JVoPvFRcCpexVKVHPlPCaaa6Yl64B7ZQFjp1oeuTKM6_aFpDxc_LhtHdO8eeKeTFjyBaHASaMazZd03DJlZKF_HQibYo5J_RmTmGE9GAYNZtVczT_WDWb1a1ZrJbpt4931n7rPc0-aSzAuxPgIRr4kUI2t9_LBkEpKwkaXoirE4HFx33AZLINOFl0IaFdjIvhv6L8ASVQm7w</recordid><startdate>2011</startdate><enddate>2011</enddate><creator>Arias, Diego G.</creator><creator>Cabeza, Matías S.</creator><creator>Erben, Esteban D.</creator><creator>Carranza, Pedro G.</creator><creator>Lujan, Hugo D.</creator><creator>Téllez Iñón, María T.</creator><creator>Iglesias, Alberto A.</creator><creator>Guerrero, Sergio A.</creator><general>Elsevier Inc</general><scope>FBQ</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></search><sort><creationdate>2011</creationdate><title>Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp</title><author>Arias, Diego G. ; Cabeza, Matías S. ; Erben, Esteban D. ; Carranza, Pedro G. ; Lujan, Hugo D. ; Téllez Iñón, María T. ; Iglesias, Alberto A. ; Guerrero, Sergio A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-49dadd549afb7355e66b7dad0f175f919371f6d2a9d7ca3e852be37f1f744ae13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>antioxidants</topic><topic>biochemical pathways</topic><topic>Cells, Cultured</topic><topic>Cercopithecus aethiops</topic><topic>Cloning, Molecular</topic><topic>developmental stages</topic><topic>electrophoresis</topic><topic>enzymes</topic><topic>Escherichia coli</topic><topic>Free radicals</topic><topic>gene expression</topic><topic>genes</topic><topic>Metabolic Detoxication, Phase I - genetics</topic><topic>Metabolic Networks and Pathways - genetics</topic><topic>methionine</topic><topic>Methionine sulfoxide</topic><topic>Methionine Sulfoxide Reductases - chemistry</topic><topic>Methionine Sulfoxide Reductases - genetics</topic><topic>Methionine Sulfoxide Reductases - isolation & purification</topic><topic>Methionine Sulfoxide Reductases - metabolism</topic><topic>Models, Molecular</topic><topic>molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>Oxidation-Reduction</topic><topic>Oxidative stress</topic><topic>Oxidative Stress - genetics</topic><topic>pathogens</topic><topic>recombinant proteins</topic><topic>Sequence Homology</topic><topic>Trypanosoma</topic><topic>Trypanosoma - enzymology</topic><topic>Trypanosoma - genetics</topic><topic>Trypanosoma brucei</topic><topic>Trypanosoma brucei brucei - enzymology</topic><topic>Trypanosoma brucei brucei - genetics</topic><topic>Trypanosoma brucei brucei - metabolism</topic><topic>Trypanosoma cruzi</topic><topic>Trypanosoma cruzi - enzymology</topic><topic>Trypanosoma cruzi - genetics</topic><topic>Trypanosoma cruzi - metabolism</topic><topic>Trypanothione</topic><topic>Tryparedoxin</topic><topic>Vero Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arias, Diego G.</creatorcontrib><creatorcontrib>Cabeza, Matías S.</creatorcontrib><creatorcontrib>Erben, Esteban D.</creatorcontrib><creatorcontrib>Carranza, Pedro G.</creatorcontrib><creatorcontrib>Lujan, Hugo D.</creatorcontrib><creatorcontrib>Téllez Iñón, María T.</creatorcontrib><creatorcontrib>Iglesias, Alberto A.</creatorcontrib><creatorcontrib>Guerrero, Sergio A.</creatorcontrib><collection>AGRIS</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><jtitle>Free radical biology & medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arias, Diego G.</au><au>Cabeza, Matías S.</au><au>Erben, Esteban D.</au><au>Carranza, Pedro G.</au><au>Lujan, Hugo D.</au><au>Téllez Iñón, María T.</au><au>Iglesias, Alberto A.</au><au>Guerrero, Sergio A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp</atitle><jtitle>Free radical biology & medicine</jtitle><addtitle>Free Radic Biol Med</addtitle><date>2011</date><risdate>2011</risdate><volume>50</volume><issue>1</issue><spage>37</spage><epage>46</epage><pages>37-46</pages><issn>0891-5849</issn><eissn>1873-4596</eissn><abstract>Methionine is an amino acid susceptible to being oxidized to methionine sulfoxide (MetSO). The reduction of MetSO to methionine is catalyzed by methionine sulfoxide reductase (MSR), an enzyme present in almost all organisms. In trypanosomatids, the study of antioxidant systems has been mainly focused on the involvement of trypanothione, a specific redox component in these organisms. However, no information is available concerning their mechanisms for repairing oxidized proteins, which would be relevant for the survival of these pathogens in the various stages of their life cycle. We report the molecular cloning of three genes encoding a putative A-type MSR in trypanosomatids. The genes were expressed in
Escherichia coli, and the corresponding recombinant proteins were purified and functionally characterized. The enzymes were specific for L-Met(
S)SO reduction, using
Trypanosoma cruzi tryparedoxin I as the reducing substrate. Each enzyme migrated in electrophoresis with a particular profile reflecting the differences they exhibit in superficial charge. The in vivo presence of the enzymes was evidenced by immunological detection in replicative stages of
T. cruzi and
Trypanosoma brucei. The results support the occurrence of a metabolic pathway in
Trypanosoma spp. involved in the critical function of repairing oxidized macromolecules.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20969952</pmid><doi>10.1016/j.freeradbiomed.2010.10.695</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0891-5849 |
ispartof | Free radical biology & medicine, 2011, Vol.50 (1), p.37-46 |
issn | 0891-5849 1873-4596 |
language | eng |
recordid | cdi_proquest_miscellaneous_822363776 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Amino Acid Sequence Animals antioxidants biochemical pathways Cells, Cultured Cercopithecus aethiops Cloning, Molecular developmental stages electrophoresis enzymes Escherichia coli Free radicals gene expression genes Metabolic Detoxication, Phase I - genetics Metabolic Networks and Pathways - genetics methionine Methionine sulfoxide Methionine Sulfoxide Reductases - chemistry Methionine Sulfoxide Reductases - genetics Methionine Sulfoxide Reductases - isolation & purification Methionine Sulfoxide Reductases - metabolism Models, Molecular molecular cloning Molecular Sequence Data Oxidation-Reduction Oxidative stress Oxidative Stress - genetics pathogens recombinant proteins Sequence Homology Trypanosoma Trypanosoma - enzymology Trypanosoma - genetics Trypanosoma brucei Trypanosoma brucei brucei - enzymology Trypanosoma brucei brucei - genetics Trypanosoma brucei brucei - metabolism Trypanosoma cruzi Trypanosoma cruzi - enzymology Trypanosoma cruzi - genetics Trypanosoma cruzi - metabolism Trypanothione Tryparedoxin Vero Cells |
title | Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T05%3A51%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20characterization%20of%20methionine%20sulfoxide%20reductase%20A%20from%20Trypanosoma%20spp&rft.jtitle=Free%20radical%20biology%20&%20medicine&rft.au=Arias,%20Diego%20G.&rft.date=2011&rft.volume=50&rft.issue=1&rft.spage=37&rft.epage=46&rft.pages=37-46&rft.issn=0891-5849&rft.eissn=1873-4596&rft_id=info:doi/10.1016/j.freeradbiomed.2010.10.695&rft_dat=%3Cproquest_cross%3E822363776%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=822363776&rft_id=info:pmid/20969952&rft_els_id=S0891584910013183&rfr_iscdi=true |