TAILIEUCHUNG - Báo cáo khoa học: Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70 Role of the divergent C-terminal a-helical subdomain

Among the eukaryotic members of the Hsp70 family, mitochondrial Hsp70 shows the highest degree of sequence identity with bacterial DnaK. Although they share a functional mechanism and homologous co-chaper-ones, they are highly specific and cannot be exchanged betweenEscherichia coliand yeast mitochondria. | iFEBS Journal Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70 Role of the divergent C-terminal a-helical subdomain Fernando Moro1 Vanesa Fernandez-Saiz1 Olga Slutsky2 Abdussalam Azem2 and Arturo Muga1 1 Unidad de Biofisica CSIC-UPV EHU y Departamento de Bioquimica y Biologia Molecular Universidad delPais Vasco Bilbao Spain 2 George S. Wise Faculty of Sciences Department of Biochemistry TelAviv University Israel Keywords allosterism chaperones DnaK mitochondrialHsp70 Correspondence F. Moro or A. Muga Unidad de Biofisica CSIC-UPV EHU y Departamento de Bioquimica y Biologia Molecular Facultad de Ciencias Universidad delPais Vasco Apartado 644 48080 Bilbao Spain E-mail gbbmopef@ or gbpmuvia@ Received 8 April2005 revised 20 April 2005 accepted 25 April 2005 doi Among the eukaryotic members of the Hsp70 family mitochondrial Hsp70 shows the highest degree of sequence identity with bacterial DnaK. Although they share a functional mechanism and homologous co-chaper-ones they are highly specific and cannot be exchanged between Escherichia coli and yeast mitochondria. To provide a structural basis for this finding we characterized both proteins as well as two DnaK mtHsp70 chimeras constructed by domain swapping using biochemical and biophysical methods. Here we show that DnaK and mtHsp70 display different conformational and biochemical properties. Replacing different regions of the DnaK peptide-binding domain with those of mtHsp70 results in chimeric proteins that a are not able to support growth of an E. coli DnaK deletion strain at stress temperatures . 42 C b show increased accessibility and decreased thermal stability of the peptide-binding pocket and c have reduced activation by bacterial but not mitochondrial co-chaperones as compared with DnaK. Importantly swapping the C-terminal a-helical subdomain promotes a conformational change in the chimeras to an mtHsp70-like conformation. Thus .

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