HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo
Ensifer meliloti is a nitrogen-fixing symbiont of the alfalfa legume able to use heme as an iron source. The transport mechanism involved in heme acquisition in E. meliloti has been identified and characterized, but the fate of heme once inside the cell is not known. In silico analysis of E. melilot...
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Weitere Verfasser: | , , , , , |
| Format: | article |
| Sprache: | Englisch |
| Veröffentlicht: |
2016
|
| Schlagworte: | |
| Online-Zugang: | http://hdl.handle.net/20.500.12381/200 http://dx.doi.org/10.1007/s10534-016-9919-3 |
| Tags: |
Keine Tags, Fügen Sie das erste Tag hinzu!
|
| _version_ | 1868890130296602625 |
|---|---|
| author | Amarelle, Vanesa |
| author2 | Rosconi, Federico Lázaro-Mártinez, Juan Manuel Buldain, Graciela Noya, Francisco O´Brian, Mark R. Fabiano, Elena |
| author2_role | author author author author author author |
| author_browse | Amarelle, Vanesa Buldain, Graciela Fabiano, Elena Lázaro-Mártinez, Juan Manuel Noya, Francisco O´Brian, Mark R. Rosconi, Federico |
| author_facet | Amarelle, Vanesa Rosconi, Federico Lázaro-Mártinez, Juan Manuel Buldain, Graciela Noya, Francisco O´Brian, Mark R. Fabiano, Elena |
| author_role | author |
| collection | REDI |
| dc.creator.none.fl_str_mv | Amarelle, Vanesa Rosconi, Federico Lázaro-Mártinez, Juan Manuel Buldain, Graciela Noya, Francisco O´Brian, Mark R. Fabiano, Elena |
| dc.date.none.fl_str_mv | 2016 2019-11-05T20:42:32Z 2019-11-05T20:42:32Z |
| dc.format.none.fl_str_mv | 17 p. |
| dc.identifier.none.fl_str_mv | http://hdl.handle.net/20.500.12381/200 PR_FCE_2009_1_2564 http://dx.doi.org/10.1007/s10534-016-9919-3 |
| dc.language.none.fl_str_mv | eng |
| dc.publisher.none.fl_str_mv | Springer |
| dc.rights.none.fl_str_mv | Acceso abierto info:eu-repo/semantics/openAccess Reconocimiento-NoComercial-SinObraDerivada. (CC BY-NC-ND) |
| dc.source.none.fl_str_mv | BioMetals. 2016; 29(2) reponame:REDI instname:Agencia Nacional de Investigación e Innovación instacron:Agencia Nacional de Investigación e Innovación |
| dc.subject.none.fl_str_mv | Rizobios Hemo-oxigenasas Metabolismo de hierro Degradación de hemo Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| dc.title.none.fl_str_mv | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| dc.type.none.fl_str_mv | Artículo info:eu-repo/semantics/article Publicado info:eu-repo/semantics/publishedVersion |
| description | Ensifer meliloti is a nitrogen-fixing symbiont of the alfalfa legume able to use heme as an iron source. The transport mechanism involved in heme acquisition in E. meliloti has been identified and characterized, but the fate of heme once inside the cell is not known. In silico analysis of E. meliloti 1021 genome revealed no canonical heme oxygenases although two genes encoding putative heme degrading enzymes, smc01518 and hmuS, were identified. SMc01518 is similar to HmuQ of Bradyrhizobium japonicum, which is weakly homologous to the Staphylococcus aureus IsdG heme-degrading monooxygenase, whereas HmuS is homolog to Pseudomonas aeruginosa PhuS, a protein reported as a heme chaperone and as a heme degrading enzyme. Recombinant HmuQ and HmuS were able to bind hemin with a 1:1 stoichiometry and displayed a Kd value of 5 and 4 lM, respectively. HmuS degrades heme in vitro to the biliverdin isomers IX-b and IX-d in an equimolar ratio. The HmuQ recombinant protein degrades heme to biliverdin IX-d only. Additionally, in this work we demonstrate that humS and hmuQ gene expression is regulated by iron and heme in a RirA dependent manner and that both proteins are involved in heme metabolism in E. meliloti in vivo. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | anni_8e64bc31ba7b74deb6ec10ef2a7b6de9 |
| identifier_str_mv | PR_FCE_2009_1_2564 |
| instacron_str | Agencia Nacional de Investigación e Innovación |
| institution | Agencia Nacional de Investigación e Innovación |
| instname_str | Agencia Nacional de Investigación e Innovación |
| language | eng |
| network_acronym_str | anni |
| network_name_str | oai-lr-anni |
| oai_identifier_str | oai:redi.anii.org.uy:20.500.12381/200 |
| publishDate | 2016 |
| publishDateSort | 2016 |
| publisher.none.fl_str_mv | Springer |
| reponame_str | REDI |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | Acceso abierto Reconocimiento-NoComercial-SinObraDerivada. (CC BY-NC-ND) |
| spelling | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivoAmarelle, VanesaRosconi, FedericoLázaro-Mártinez, Juan ManuelBuldain, GracielaNoya, FranciscoO´Brian, Mark R.Fabiano, ElenaRizobiosHemo-oxigenasasMetabolismo de hierroDegradación de hemoCiencias Naturales y ExactasCiencias BiológicasBioquímica y Biología MolecularEnsifer meliloti is a nitrogen-fixing symbiont of the alfalfa legume able to use heme as an iron source. The transport mechanism involved in heme acquisition in E. meliloti has been identified and characterized, but the fate of heme once inside the cell is not known. In silico analysis of E. meliloti 1021 genome revealed no canonical heme oxygenases although two genes encoding putative heme degrading enzymes, smc01518 and hmuS, were identified. SMc01518 is similar to HmuQ of Bradyrhizobium japonicum, which is weakly homologous to the Staphylococcus aureus IsdG heme-degrading monooxygenase, whereas HmuS is homolog to Pseudomonas aeruginosa PhuS, a protein reported as a heme chaperone and as a heme degrading enzyme. Recombinant HmuQ and HmuS were able to bind hemin with a 1:1 stoichiometry and displayed a Kd value of 5 and 4 lM, respectively. HmuS degrades heme in vitro to the biliverdin isomers IX-b and IX-d in an equimolar ratio. The HmuQ recombinant protein degrades heme to biliverdin IX-d only. Additionally, in this work we demonstrate that humS and hmuQ gene expression is regulated by iron and heme in a RirA dependent manner and that both proteins are involved in heme metabolism in E. meliloti in vivo.Agencia Nacional de Investigación e InnovaciónSpringer2019-11-05T20:42:32Z2019-11-05T20:42:32Z2016Artículoinfo:eu-repo/semantics/articlePublicadoinfo:eu-repo/semantics/publishedVersion17 p.http://hdl.handle.net/20.500.12381/200PR_FCE_2009_1_2564http://dx.doi.org/10.1007/s10534-016-9919-3BioMetals. 2016; 29(2)reponame:REDIinstname:Agencia Nacional de Investigación e Innovacióninstacron:Agencia Nacional de Investigación e InnovaciónengAcceso abiertoinfo:eu-repo/semantics/openAccessReconocimiento-NoComercial-SinObraDerivada. (CC BY-NC-ND)oai:redi.anii.org.uy:20.500.12381/2002026-06-16T05:02:45Z |
| spellingShingle | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo Amarelle, Vanesa Rizobios Hemo-oxigenasas Metabolismo de hierro Degradación de hemo Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| status_str | publishedVersion |
| title | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| title_full | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| title_fullStr | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| title_full_unstemmed | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| title_short | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| title_sort | HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo |
| topic | Rizobios Hemo-oxigenasas Metabolismo de hierro Degradación de hemo Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| url | http://hdl.handle.net/20.500.12381/200 http://dx.doi.org/10.1007/s10534-016-9919-3 |