J Cell Biol 1999,
PMID: 10477748
Kickhoefer, V A; Siva, A C; Kedersha, N L; Inman, E M; Ruland, C; Streuli, M; Rome, L H
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 approximately 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.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Biogrid Interaction:
PARP4
—
MVP
(direct interaction, two hybrid)
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IRef Biogrid Interaction:
PARP4
—
MVP
(direct interaction, pull down)
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Gene Ontology Complexes spindle microtubule:
spindle microtubule complex (AURKC-BIRC8-NUMA1-BIRC7-ARL3-CALM1-BIRC3-KIF4A-SKA1-PARP4-XIAP-SKA2-KIF11-KIFAP3-NEIL2-NLRC4-CAPN6-KIF3A-KIF3B-TUBG2)
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IRef Hprd Interaction:
PARP4
—
MVP
(two hybrid)
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IRef Hprd Interaction:
PARP4
—
MVP
(in vitro)
-
IRef Hprd Interaction:
PARP4
—
MVP
(in vivo)
In total, 191 gene pairs are associated to this article in curated databases