The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase

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  • Valerie A. Kickhoefer
    aDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737
  • Amara C. Siva
    aDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737
  • Nancy L. Kedersha
    bDivision of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, Massachusetts 02115
  • Elisabeth M. Inman
    aDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737
  • Cristina Ruland
    aDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737
  • Michel Streuli
    cDepartment of Cancer, Immunology, and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115
  • Leonard H. Rome
    aDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737

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<jats:p>Mammalian vaults are ribonucleoprotein (RNP) complexes, composed of a small ribonucleic acid and three proteins of 100, 193, and 240 kD in size. The 100-kD major vault protein (MVP) accounts for &gt;70% of the particle mass. We have identified the 193-kD vault protein by its interaction with the MVP in a yeast two-hybrid screen and confirmed its identity by peptide sequence analysis. Analysis of the protein sequence revealed a region of ∼350 amino acids that shares 28% identity with the catalytic domain of poly(ADP-ribose) polymerase (PARP). PARP is a nuclear protein that catalyzes the formation of ADP-ribose polymers in response to DNA damage. The catalytic domain of p193 was expressed and purified from bacterial extracts. Like PARP, this domain is capable of catalyzing a poly(ADP-ribosyl)ation reaction; thus, the 193-kD protein is a new PARP. Purified vaults also contain the poly(ADP-ribosyl)ation activity, indicating that the assembled particle retains enzymatic activity. Furthermore, we show that one substrate for this vault-associated PARP activity is the MVP. Immunofluorescence and biochemical data reveal that p193 protein is not entirely associated with the vault particle, suggesting that it may interact with other protein(s). A portion of p193 is nuclear and localizes to the mitotic spindle.</jats:p>

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