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The ubiquitous Heat shock protein 70 (HSP70) family consists of ATP-dependent chaperones that perform many cellular functions that affect almost all aspects of the protein life cycle, from biosynthesis to degradation [1-3
].
Recently, two articles on the mechanism of HSP70 functional diversity regulation were published on Nature, namely the Rina Rosenzweig research group of the Weizmann Institute of Scientific Research in Israel and the Bernd Bukau research group of the German DKFZ-ZMBH alliance published an article entitled HSP40 proteins use class-specific regulation to drive HSP70 functional Persity and the German DKFZ-ZMBH Consortium Bernd Bukau Research Group and Anne S.
The proteins of the JDPs family are interesting because, although the proteins in this family are structurally similar (Figure 1), their functions within the cell are very different
。 For example, the domain composition of JDPs in Class A and Class B families is very similar, and the affinity between amyloid fibres such as α-synuclein and Tau proteins is similar, but only JDPs of Class B can effectively promote the depolymerization of amyloid fibers together with HSP70 as comolecular chaperones [4,5], involving the specific mechanisms involved and the basis of molecular biology is unknown
。
Figure 1 Schematic diagram of JDPs domains of Class A and Class B families
To unravel the specific mechanism by which Class A and Class B JDPs proteins diverge in function, the authors used nuclear magnetic resonance to analyze
the binding of two family proteins to HSP70.
The authors found that Class B's JDPs include an additional HSP70 binding site in addition to the inherent suppression domain, and the GF suppression domain and the second HSP70 binding site are two special domains that are not available in Class A's
JDPs.
Overall, the two back-to-back Nature articles uncover specific molecular mechanisms
by which the HSP70 protein family performs a wide range of biological functions.
