Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis

J Biol Chem. 2006 Dec 8;281(49):37888-92. doi: 10.1074/jbc.M608147200. Epub 2006 Oct 11.

Abstract

HSPA2 (formerly HSP70.2) is a testis-specific member of the HSP70 family known to play a critical role in the completion of meiosis during male germ cell differentiation. Although abundantly present in post-meiotic cells, its function during spermiogenesis remained obscure. Here, using a global proteomic approach to identify genome-organizing proteins in condensing spermatids, we discovered an unexpected role for HSPA2, which acquires new functions and becomes tightly associated with major spermatid DNA-packaging proteins, transition proteins 1 and 2. Hence, HSPA2 is identified here as the first transition protein chaperone, and these data shed a new light on the yet totally unknown process of genome-condensing structure assembly in spermatids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromosomal Proteins, Non-Histone / metabolism
  • DNA Packaging
  • DNA-Binding Proteins
  • HSP70 Heat-Shock Proteins / metabolism*
  • In Vitro Techniques
  • Male
  • Meiosis
  • Mice
  • Nuclear Proteins / metabolism
  • Protein Binding
  • Proteomics
  • Spermatids / cytology
  • Spermatids / metabolism
  • Spermatogenesis / physiology*

Substances

  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • HSP70 Heat-Shock Proteins
  • Hspa2 protein, mouse
  • Nuclear Proteins
  • Tnp2 protein, mouse
  • spermatid transition proteins