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      Polypyrimidine tract binding protein 2 stabilizes phosphoglycerate kinase 2 mRNA in murine male germ cells by binding to its 3'UTR.

      Biology of reproduction
      Animals, Gene Expression Profiling, Germ Cells, metabolism, HeLa Cells, Humans, Isoenzymes, physiology, Male, Mice, Mice, Inbred Strains, Nerve Tissue Proteins, genetics, Phosphoglycerate Kinase, Polypyrimidine Tract-Binding Protein, Protein Binding, RNA Stability, RNA, Messenger, RNA-Binding Proteins, Regulatory Elements, Transcriptional, Spermatozoa, Testis, chemistry, Transfection

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          Abstract

          The mRNA that encodes the testis-specific protein phosphoglycerate kinase (PGK2) is a long-lived mRNA that is transcribed in meiotic and postmeiotic male germ cells. Pgk2 mRNA is present in germ cells for up to 2 wk before its protein product is detected. Using affinity chromatography with the 3'-UTR of the Pgk2 mRNA, several proteins, including the RNA-binding protein, polypyrimidine tract binding protein 2 (PTBP2), were identified in mouse testis extracts. Coimmunoprecipitation experiments confirmed that PTBP2 binds to Pgk2 mRNA in the testis and RNA gel shifts demonstrated that PTBP2, but not PTBP1, binds to a specific region of the Pgk2 3'-UTR. Recombinant PTBP2 increased the stability of reporter constructs that contained the 3'-UTR Pgk2 sequence element in both testis extracts and transfected HeLa cells. We propose that PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells.

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