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Vertebrate mono-ADP-ribosyltransferases

  • Part III Mono(ADP-ribosylation)
  • A. ADP-ribosylation Cycle
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Mono-ADP-ribosylation appears to be a reversible modification of proteins, which occurs in many eukaryotic and prokaryotic organisms. Multiple forms of arginine-specific ADP-ribosyltransferases have been purified and characterized from avian crythrocytes, chicken polymorphonuclear leukocytes and mammalian skeletal muscle. The avian transferases have similar molecular weights of∼28 kDa, but differ in physical, regulatory and kinetic properties and subcellular localization. Recently, a 38-kDa rabbit skeletal muscle ADP-ribosyltransferase was purified and cloned. The deduced amino acid sequence contained hydrophobic amino and carboxy termini, consistent with known signal sequences of glycosylphosphatidylinositol (GPI)-anchored proteins. This arginine-specific transferase was present on the surface of mouse myotubes and of NMU cells transfected with the cDNA and was released with phosphatidylinositol-specific phospholipase C. Arginine-specific ADP-ribosyltransferases thus appear to exhibit considerable diversity in their structure, cellular localization, regulation and physiological role.

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  1. Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 10, Room 5N-307, 9000, 20892, Rockville Pike, Bethesda, Maryland, USA

    Anna Zolkiewska, Ian J. Okazaki & Joel Moss

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  1. Anna Zolkiewska
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  2. Ian J. Okazaki
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  3. Joel Moss
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Zolkiewska, A., Okazaki, I.J. & Moss, J. Vertebrate mono-ADP-ribosyltransferases. Mol Cell Biochem 138, 107–112 (1994). https://doi.org/10.1007/BF00928450

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