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La protine chaperon dEscherichia coli DnaK est la protine de choc thermique de 70 kDa (HSP70) la mieux caractrise. Ces chaperons molculaires exercent leur fonction principale grce des cycles successifs de fixation et de libration des polypeptides, coupls des cycles dhydrolyse de l'ATP sous le contrle de cofacteurs protiques. Trs similaires au niveau de leur structure, les nombreuses HSP70s diffrent pourtant en termes de spcificit de substrat et dinteraction. Afin de dterminer les bases structurales de cette spcificit, des tudes de complmentation ont t ralises en utilisant des protines chimres composes de diffrentes combinaisons entre les domaines respectifs de DnaK et ceux de son homologue Hsc70 de rat. Les rsultats obtenus montrent que seules les chimres possdant le domaine de fixation des peptides de DnaK sont capables de restaurer les phnotypes sauvages et que le sousdomaine B, portant le site de fixation des peptides substrats, est le responsable de la spcificit de fonction de DnaK chez E.coli. Ces rsultats bousculent certaines ides reues sur le mode de fonctionnement des HPS70s et offrent de nombreuses perspectives de recherche.
⚠️ WARNING (California Proposition 65):
This product may contain chemicals known to the State of California to cause cancer,
birth defects, or other reproductive harm.
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