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© The Rockefeller University Press, 0021-9525/1999/9/917/ $5.00
The Journal of Cell Biology, Volume 146, Number 5, September 6, 1999 917-928

The 193-kD Vault Protein, VPARP, Is a Novel Poly(ADP-ribose) Polymerase

Valerie A. Kickhoefera, Amara C. Sivaa, Nancy L. Kedershab, Elisabeth M. Inmana, Cristina Rulanda, Michel Streulic, and Leonard H. Romea
a Department of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, California 90095-1737
b Division of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, Massachusetts 02115
c Department of Cancer, Immunology, and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115

Correspondence to: Valerie A. Kickhoefer, 33-257 CHS, Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, CA 90095-1737. Tel:(310) 825-0397 Fax:(310) 206-5272 E-mail:vkick{at}mednet.ucla.edu.

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 >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.

Key Words: vaults, ribonucleoprotein particle, poly(ADP-ribose) polymerase, poly(ADP-ribose), mitotic spindle


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