HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo

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• 作者：Vanesa Amarelle ; Federico Rosconi ; Juan Manuel Lázaro-Martínez…
• 关键词：Rhizobia ; Heme ; oxygenase ; Iron metabolism ; Heme ; E. meliloti ; Heme ; degradation
• 刊名：Biometals
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：29
• 期：2
• 页码：333-347
• 全文大小：1,113 KB
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• 作者单位：Vanesa Amarelle (1)
  Federico Rosconi (1)
  Juan Manuel Lázaro-Martínez (2)
  Graciela Buldain (2)
  Francisco Noya (1)
  Mark R. O’Brian (3)
  Elena Fabiano (1)
  
  1. Biochemical and Microbial Genomics Department, Instituto de Investigaciones Biológicas Clemente Estable, MEC, Montevideo, Uruguay
  2. CONICET and Faculty of Pharmacy and Biochemistry, Universidad de Buenos Aires, Buenos Aires, Argentina
  3. State University of New York at Buffalo, New York, USA
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Physical Chemistry
  
• 出版者：Springer Netherlands
• ISSN：1572-8773

文摘

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 K_d value of 5 and 4 µM, respectively. HmuS degrades heme in vitro to the biliverdin isomers IX-β and IX-δ in an equimolar ratio. The HmuQ recombinant protein degrades heme to biliverdin IX-δ 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.