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Structural insights into the formation of oligomeric state by a type I Hsp40 chaperone.

Zhu M, Ou D, Khan MH, Zhao S, Zhu Z, Niu L
Biochimie 176 45-51 (2020)
Cited: 3 times
EuropePMC logo PMID: 32621942

Abstract

Molecular chaperones can prevent and repair protein misfolding and aggregation to maintain protein homeostasis in cells. Hsp40 chaperones interact with unfolded client proteins via the dynamic multivalent interaction (DMI) mechanism with their multiple client-binding sites. Here we report that a type I Hsp40 chaperone from Streptococcus pneumonia (spHsp40) forms a concentration-independent polydispersity oligomer state in solution. The crystal structure of spHsp40 determined at 2.75 Å revealed that each monomer has a type I Hsp40 structural fold containing a zinc finger domain and C-terminal domains I and II (CTD I and CTD II). Subsequent quaternary structure analysis using a PISA server generated two dimeric models. The interface mutational analysis suggests the conserved C-terminal dimeric motif as a basis for dimer formation and that the novel dimeric interaction between a client-binding site in CTD I and the zinc finger domain promotes the formation of the spHsp40 oligomeric state. In vitro functional analysis demonstrated that spHsp40 oligomer is fully active and possess the optimal activity in stimulating the ATPase activity of spHsp70. The oligomer state of type I Hsp40 and its formation might be important in understanding Hsp40 function and its interaction with client proteins.

Articles - 6jzb mentioned but not cited (1)

  1. Evolution and activation mechanism of the flavivirus class II membrane-fusion machinery. Vaney MC, Dellarole M, Duquerroy S, Medits I, Tsouchnikas G, Rouvinski A, England P, Stiasny K, Heinz FX, Rey FA. Nat Commun 13 3718 (2022)


Articles citing this publication (2)

  1. Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone. Roterman I, Stapor K, Konieczny L. BMC Bioinformatics 24 418 (2023)
  2. The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70. Velasco-Carneros L, Cuéllar J, Dublang L, Santiago C, Maréchal JD, Martín-Benito J, Maestro M, Fernández-Higuero JÁ, Orozco N, Moro F, Valpuesta JM, Muga A. Nat Commun 14 5436 (2023)


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