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Relation Structure-Fonction de la Protéine Chaperon Dnak: (Omn.Pres.Franc.)

Relation Structure-Fonction de la Protéine Chaperon Dnak: (Omn.Pres.Franc.)


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La protéine chaperon d'Escherichia coli DnaK est la protéine de choc thermique de 70 kDa (HSP70) la mieux caractérisée. Ces chaperons moléculaires exercent leur fonction principale grâce à des cycles successifs de fixation et de libération des polypeptides, couplés à des cycles d'hydrolyse de l'ATP sous le contrôle de co-facteurs protéiques. Très similaires au niveau de leur structure, les nombreuses HSP70s diffèrent pourtant en termes de spécificité de substrat et d'interaction. Afin de déterminer les bases structurales de cette spécificité, des études de complémentation ont été réalisées en utilisant des protéines chimères composées de différentes combinaisons entre les domaines respectifs de DnaK et ceux de son homologue Hsc70 de rat. Les résultats obtenus montrent que seules les chimères possédant le domaine de fixation des peptides de DnaK sont capables de restaurer les phénotypes sauvages et que le sous-domaine B, portant le site de fixation des peptides substrats, est le responsable de la spécificité de fonction de DnaK chez E.coli. Ces résultats bousculent certaines idées reçues sur le mode de fonctionnement des HPS70s et offrent de nombreuses perspectives de recherche.


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Product Details
  • ISBN-13: 9783838170435
  • Publisher: Omniscriptum
  • Publisher Imprint: Omniscriptum
  • Height: 229 mm
  • No of Pages: 188
  • Returnable: N
  • Spine Width: 11 mm
  • Width: 152 mm
  • ISBN-10: 3838170431
  • Publisher Date: 28 Feb 2018
  • Binding: Paperback
  • Language: French
  • Returnable: N
  • Series Title: Omn.Pres.Franc.
  • Weight: 331 gr


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