KIN17 encodes an RNA-binding protein and is expressed during mouse spermatogenesis

Author:

Pinon-Lataillade Ghislaine1,Masson Christel1,Bernardino-Sgherri Jacqueline2,Henriot Véronique1,Mauffrey Philippe1,Frobert Yveline3,Araneda Silvia4,Angulo Jaime F.1

Affiliation:

1. Laboratoire de Génétique de la Radiosensibilité, CEA, Direction des Sciences du Vivant (DSV), Département de Radiobiologie et de Radiopathologie (DRR), B.P. 6, 92265 Fontenay aux Roses CEDEX, France

2. Laboratoire de la Radiosensibilité des Cellules Germinales, CEA, DSV, DRR, U 566 CEA-INSERM-Université Paris VII, B.P. 6, 92265 Fontenay aux Roses CEDEX, France

3. Service de Pharmacologie et d'Immunologie, Département de Recherche Médicale, DSV, CEA-Saclay, 91191 Gif-sur Yvette, France

4. Physiologie Integrative, Cellulaire et Moléculaire, UMR 5123 CNRS/UCB Lyon 1, 43 Bd. 11 novembre 1918, 69622 Villeurbanne CEDEX, France

Abstract

Genotoxic agents deform DNA structure thus eliciting a complex genetic response allowing recovery and cell survival. The Kin17 gene is up-regulated during this response. This gene encodes a conserved nuclear protein that shares a DNA-binding domain with the bacterial RecA protein. The KIN17 protein binds DNA and displays enhanced expression levels in proliferating cultured cells, suggesting a role in nuclear metabolism. We investigated this by studying the expression profile of KIN17 protein during mouse spermatogenesis. As expected, the expression level of Kin17 is higher in proliferating than in differentiated cells. KIN17 is selectively extracted from this tissue by detergents and a fraction was tightly associated with the nuclear matrix. Germinal cells ubiquitously express Kin17 and the protein is located mainly in the nucleus except in elongated spermatids where cytoplasmic staining is also observed. Sertoli and germ cells that are no longer mitotically active express KIN17, suggesting a general role in all testicular cell types. In adult testis a significant proportion of KIN17 co-purifies with polyadenylated RNA. KIN17 directly binds RNA, preferentially poly(G) and poly(U) homopolymers. These results together with the identification of KIN17 as a component of the human spliceosome indicate that this protein may participate in RNA processing.

Publisher

The Company of Biologists

Subject

Cell Biology

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