Aug 21, 2014

Structural influence of the conserved Hsp40 HPD tripeptide on Hsp70 chaperone function

bioRxiv
Cristina Gutiérrez-CaballeroStephen J Royle

Abstract

The control of Hsp70 functions has been related to the modulation of ATP hydrolysis and substrate capture by Hsp40. Structural and biophysical analyses of Hsp40 variants and their interactions with Hsp70 have identified key residues for this functional control mechanism. Conserved residues in both Hsp40 and Hsp70 have revealed conserved interactions that link Hsp40 binding to the catalytic residues within Hsp70. The current work investigates the effect of documented J-domain dysfunctional mutations (i.e. D35N, H33Q) on the described interaction linkage. Molecular dynamics simulations were used to compare the persistence of individual bond types (i.e. H-bonds, salt bridges, hydrophobic interactions) between Hsp70 and the bound forms of functional and dysfunctional Hsp40 variants. The generated data suggests the involvement of both direct and allosteric effects for the tested mutations. The observed changes relate mutations in the conserved HPD tripeptide of Hsp40 to alterations in the interaction network that induces Hsp70 chaperone functions.

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Mentioned in this Paper

Transforming Acidic Coiled-Coil Containing Protein 3
Polymerase
Post-Translational Protein Processing
Mitotic Spindle Apparatus
Spindle Microtubule
Ch-TOG protein, human
TACC3 gene
Protein Phosphorylation
Centrosome
Coiled-Coil Domain

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