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The 193-Kd VaultProtein, Vparp, Is aNovelPoly(Adp-Ribose)Polymerase Valerie A. KickhoeferAmara C. SivaNancy Kedersha1999 год

The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
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Аннотация: 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.
Год издания: 1999
Авторы: Valerie A. Kickhoefer, Amara C. Siva, Nancy Kedersha, Elisabeth M. Inman, Cristina T. Ruland, Michel Streuli, Leonard H. Rome
Издательство: Rockefeller University Press
Источник: The Journal of Cell Biology
Ключевые слова: PARP inhibition in cancer therapy, DNA Repair Mechanisms, Nuclear Structure and Function
Другие ссылки: The Journal of Cell Biology (HTML)
Europe PMC (PubMed Central) (PDF)
Europe PMC (PubMed Central) (HTML)
PubMed Central (HTML)
eScholarship (California Digital Library) (PDF)
eScholarship (California Digital Library) (HTML)
PubMed (HTML)