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1 August 2001 MSJ-1, a Mouse Testis-Specific DnaJ Protein, Is Highly Expressed in Haploid Male Germ Cells and Interacts with the Testis-Specific Heat Shock Protein Hsp70-2
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Abstract

The MSJ-1 gene encodes a murine DnaJ homologue that is expressed specifically in adult testis. DnaJ proteins act as cochaperones of Hsp70 proteins in promoting diverse cellular functions. In this study we used recombinant MSJ-1 proteins to produce MSJ-1 antiserum and to carry out in vitro binding assays. In a wide immunoscreening of mouse tissues, affinity-purified MSJ-1 antibodies recognize a unique protein of 30 kDa in male germ cells only. MSJ-1 is able to interact with the testis-specific Hsp70-2 protein and can be coimmunoprecipitated with Hsp70-2 from spermatogenic cells; binding of these two chaperones is consistent with the presence of a third component, which is so far unknown. MSJ-1 is weakly detected in early round spermatids, and its protein content increases in cytodifferentiating spermatids where it colocalizes with the developing acrosome and their postnuclear region. Hsp70-2, which is known to be highly expressed in meiotic cells, shows a subcellular localization in late differentiating spermatids that overlaps that of MSJ-1. MSJ-1 is also maintained in testicular and epididymal spermatozoa, where it sharply demarcates into two distinct cell areas; the outer surface of the acrosomal vesicle, and the centrosomal area. On the whole, our findings are consistent with a role for MSJ-1 in acrosome formation and centrosome adjustment during spermatid development, whereas its presence in mature spermatozoa suggests a special function during fertilization, shortly afterward, or both.

Giovanna Berruti and Enzo Martegani "MSJ-1, a Mouse Testis-Specific DnaJ Protein, Is Highly Expressed in Haploid Male Germ Cells and Interacts with the Testis-Specific Heat Shock Protein Hsp70-2," Biology of Reproduction 65(2), 488-495, (1 August 2001). https://doi.org/10.1095/biolreprod65.2.488
Received: 8 December 2000; Accepted: 1 March 2001; Published: 1 August 2001
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