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Low serum PON1 activity: an independent risk factor for coronary artery disease in North-West Indian type 2 diabetics
Authors:Gupta Nidhi  Binu K B K  Singh Surjit  Maturu Nagarjuna V  Sharma Yash P  Bhansali Anil  Gill Kiran Dip
Affiliation:
  • a Graduate School of Environment and Information Science, Yokohama National University, Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan
  • b Interdisciplinary Research Center, Yokohama National University, Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan
  • c Laboratory of Molecular Biology, Faculty of Engineering Science, Yokohama National University, Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan
  • Abstract:Posttranslational modifications of proteins have profound effects on many aspects of their function and have received much attention due to the importance of these processes in epigenetic regulation. In this study, we report that deleted azoospermia associated protein 1 (DAZAP1)/proline-rich RNA binding protein (Prrp), a multifunctional RNA binding protein which is essential for spermatogenesis and normal cell growth, is acetylated at Lysine 150 within its RNA binding domain. The acetylation is predominantly observed in nuclear Prrp, and the nonacetylated form is in cytoplasm. Considering that Prrp is a shuttling protein, we suggest that the acetylation cycle at Prrp K150 regulates nucleocytoplasmic transport in cells.
    Keywords:anti-panAcK, Anti-pan-specific acetylated-lysine   K150, Lysine 150   MoAb, monoclonal antibody   NLS, nuclear localization signal   PEI, polyethylenimine   Prrp, proline-rich RNA binding protein   PTM, posttranslational modification   RRM, RNA recognition motif
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