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Concerted Up-regulation of Aldehyde/Alcohol Dehydrogenase (ADHE) and Starch in Chlamydomonas reinhardtii Increases Survival under Dark Anoxia

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  • معلومة اضافية
    • Contributors:
      Laboratoire de Biotechnologie de l'Environnement Narbonne (LBE); Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro); Bioénergétique et Ingénierie des Protéines (BIP); Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS); Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038); Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 )-Institut de Recherche Interdisciplinaire de Grenoble (IRIG); Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA); MICROSCOPY CORE FACILITY (IMM); Centre National de la Recherche Scientifique (CNRS); Institut de biologie physico-chimique (IBPC (FR_550)); Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS); ANR-10-INBS-08-01, ANR-10-BIOE-0004; ANR-10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010); ANR-10-BIOE-0004,Algo-H2,Optimisations génétiques, métaboliques, et procédé de la photobioproduction d'hydrogène par la microalgue verte Chlamydomonas reinhardtii(2010)
    • بيانات النشر:
      CCSD
      American Society for Biochemistry and Molecular Biology
    • الموضوع:
      2017
    • Collection:
      Aix-Marseille Université: HAL
    • نبذة مختصرة :
      International audience ; Aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate, and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes, where their physiological role and regulation are however largely unknown. Herein we provide the first molecular and enzymatic characterization of the ADHE from the photosynthetic microalga Chlamydomonas reinhardtii. Purified recombinant ADHE catalyzed the reversible NADH-mediated interconversions of acetyl-CoA, acetaldehyde and ethanol, but seemed to be poised towards the production of ethanol from acetaldehyde. Phylogenetic analysis of the algal fermentative enzyme supports a vertical inheritance from a cyanobacterial-related ancestor. ADHE was located in the chloroplast where it associated in dimers and higher order oligomers. Electron microscopy analysis of ADHE-enriched stromal fractions revealed fine spiral structures, similar to bacterial ADHE spirosomes. Protein blots showed that ADHE is regulated under oxic conditions. Upregulation is observed in cells exposed to diverse physiological stresses, including zinc deficiency, nitrogen starvation, and inhibition of carbon concentration/fixation capacity. Analyses of the overall proteome and fermentation profiles revealed that cells with increased ADHE abundance exhibit better survival under dark anoxia. This likely relates to the fact that greater ADHE abundance appeared to coincide with enhanced starch accumulation, which might reflect ADHE-mediated anticipation of anaerobic survival.
    • ISBN:
      978-0-00-395530-9
      0-00-395530-3
    • Relation:
      info:eu-repo/semantics/altIdentifier/pmid/28007962; PRODINRA: 387753; PUBMED: 28007962; WOS: 000395530300029
    • الرقم المعرف:
      10.1074/jbc.M116.766048
    • الدخول الالكتروني :
      https://amu.hal.science/hal-01430308
      https://amu.hal.science/hal-01430308v1/document
      https://amu.hal.science/hal-01430308v1/file/0130308%20vanLis_JBC_2017.pdf
      https://doi.org/10.1074/jbc.M116.766048
    • Rights:
      http://hal.archives-ouvertes.fr/licences/copyright/ ; info:eu-repo/semantics/OpenAccess
    • الرقم المعرف:
      edsbas.ADC45671