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5′-ADP-3″Deoxypentos-2″-Ulose. A Novel Product of ADP-Ribosyl Protein Lyase

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Book cover ADP-Ribosylation of Proteins

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

Our previous studies [1, 2] revealed that the degradation of poly(ADP-ribosyl) proteins is carried out by consecutive actions of two enzymes, poly(ADP-ribose) glycohydrolase [3, 4] and ADP-ribosyl protein lyase (formerly termed ADP-ribosyl histone splitting enzyme) [5] (Fig. 1). The latter enzyme catalyzes removal of the last proximal ADP-ribosyl residue from acceptor protein. This report presents, after a brief review of ADP-ribosyl histones and the lyase, the identification of the enzymatic split product as a novel sugar derivative, and discusses its significance in poly(ADP-ribosyl) protein metabolism.

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Abbreviations

FT-IR:

Fourier Transformed Infrared Spectrogram

GC/MS:

Gas Chromatography/Mass Spectrometry

HPLC:

High Performance Liquid Chromatography

References

  1. Ueda K, Kawaichi M, Oka J, Hayaishi O (1980) Biosynthesis and degradation of poly(ADP-ribosyl) histones. In: Smulson M, Sugimura T (eds) Novel ADP-ribosylations of regulatory enzymes and proteins. Elsevier/North Holland, Amsterdam New York, pp 47–56

    Google Scholar 

  2. Ueda K, Ogata N, Kawaichi M, Inada S, Hayaishi O (1982) ADP-ribosylation reactions. Cur Top Cell Regul 21:175–187

    CAS  Google Scholar 

  3. Ueda K, Oka J, Narumiya S, Miyakawa N, Hayaishi O (1972) Poly ADP-ribose glycohydrolase from rat liver nuclei, a novel enzyme degrading the polymer. Biochem Biophys Res Commun 46:516–523

    Article  PubMed  CAS  Google Scholar 

  4. Miwa M, Tanaka M, Matsushima T, Sugimura T (1974) Purification and properties of a glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose). J Biol Chem 249:3475–3482

    PubMed  CAS  Google Scholar 

  5. Okayama H, Honda M, Hayaishi O (1978) Novel enzyme from rat liver that cleaves an ADP-ribosyl histone linkage. Proc Natl Acad Sci USA 75:2254–2257

    Article  PubMed  CAS  Google Scholar 

  6. Ueda K, Hayaishi O (1985) ADP-ribosylation. Annu Rev Biochem 54:71–99

    Article  Google Scholar 

  7. Riquelme PT, Burzio LO, Koide SS (1979) ADP ribosylation of rat liver lysine-rich histone in vitro. J Biol Chem 254:3018–3028

    PubMed  CAS  Google Scholar 

  8. Ogata N, Ueda K, Hayaishi O (1980) ADP-ribosylation sites of histones H1 and H2B. In: Smulson M, Sugimura T (eds) Novel ADP-ribosylations of regulatory enzymes and proteins. Elsevier/North Holland, Amsterdam New York, pp 333–342

    Google Scholar 

  9. Ogata N, Ueda K, Kagamiyama H, Hayaishi O (1980) ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14 and COOH-terminal lysine residue as modification sites. J Biol Chem 255:7616–7620

    PubMed  CAS  Google Scholar 

  10. Burzio LO, Riquelme PT, Koide SS (1979) ADP ribosylation of rat liver nucleosomal core histories. J Biol Chem 254:3029–3037

    PubMed  CAS  Google Scholar 

  11. Ogata K, Ueda K, Hayaishi O (1980) ADP-ribosylation of historie H2B. Identification of glutamic acid residue 2 as the modification site. J Biol Chem 255:7610–7615

    PubMed  CAS  Google Scholar 

  12. Oka J, Ueda K, Hayaishi O, Komura H, Nakanishi K (1984) ADP-ribosyl protein lyase. Purification, properties, and identification of the product. J Biol Chem 259:986–995

    PubMed  CAS  Google Scholar 

  13. Kun E, Chang ACY, Sharma ML, Ferro AM, Nitecki D (1976) Covalent modification of proteins by metabolites of NAD. Proc Natl Acad Sci USA 73:3131–3135

    Article  PubMed  CAS  Google Scholar 

  14. Moss J, Vaughan M (1978) Isolation of an avian erythrocyte protein possessing ADP-ribosyl-transferase activity and capable of activating adenylate cyclase. Proc Natl Acad Sci USA 75:3621–3624

    Article  PubMed  CAS  Google Scholar 

  15. Komura H, Iwashita T, Naoki H, Nakanishi K, Oka J, Ueda K, Hayaishi O (1983) Structure and synthesis of 3-deoxy-D-glycero-pentos-2-ulose, an unusual sugar produced enzymatically from (ADP-ribosyl)histone H2B. J Am Chem Soc 105:5164–5165

    Article  CAS  Google Scholar 

  16. Wielckens K, Schmidt A, George E, Bredehorst R, Hilz H (1982) DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins. J Biol Chem 257:12872–12877

    PubMed  CAS  Google Scholar 

  17. Williams JC, Chambers JP, Liehr JG (1984) Glutamyl ribose 5-phosphate storage disease. A hereditary defect in the degradation of poly(ADP-ribosylated) proteins. J Biol Chem 259: 1037–1042

    PubMed  CAS  Google Scholar 

  18. Williams JC, Butler IJ, Rosenberg HS, Verani R, Scott CI, Conley SB (1984) Progressive neurologic deterioration and renal failure due to storage of glutamyl ribose-5-phosphate. N Engl J Med 311:152–155

    Article  PubMed  CAS  Google Scholar 

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© 1985 Springer-Verlag Berlin Heidelberg

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Ueda, K., Hayaishi, O., Oka, J., Komura, H., Nakanishi, K. (1985). 5′-ADP-3″Deoxypentos-2″-Ulose. A Novel Product of ADP-Ribosyl Protein Lyase. In: Althaus, F.R., Hilz, H., Shall, S. (eds) ADP-Ribosylation of Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70589-2_22

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  • DOI: https://doi.org/10.1007/978-3-642-70589-2_22

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-70591-5

  • Online ISBN: 978-3-642-70589-2

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