PMID- 10477748
OWN - NLM
STAT- MEDLINE
DCOM- 19991014
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 146
IP  - 5
DP  - 1999 Sep 6
TI  - The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase.
PG  - 917-28
AB  - 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.
FAU - Kickhoefer, V A
AU  - Kickhoefer VA
AD  - Department of Biological Chemistry, University of California, Los Angeles School 
      of Medicine, Los Angeles, California 90095-1737, USA. vkick@medne.tucla.edu
FAU - Siva, A C
AU  - Siva AC
FAU - Kedersha, N L
AU  - Kedersha NL
FAU - Inman, E M
AU  - Inman EM
FAU - Ruland, C
AU  - Ruland C
FAU - Streuli, M
AU  - Streuli M
FAU - Rome, L H
AU  - Rome LH
LA  - eng
SI  - GENBANK/AF158255
GR  - CA55547/CA/NCI NIH HHS/United States
GR  - GM38097/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Alpha-Globulins)
RN  - 0 (BRCA1 Protein)
RN  - 0 (Peptide Fragments)
RN  - 0 (Poly(ADP-ribose) Polymerase Inhibitors)
RN  - 0 (RNA, Messenger)
RN  - 0 (Vault Ribonucleoprotein Particles)
RN  - 0 (major vault protein)
RN  - 39346-44-6 (inter-alpha-inhibitor)
RN  - EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
SB  - IM
MH  - Alpha-Globulins/chemistry/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - BRCA1 Protein/chemistry/genetics
MH  - COS Cells
MH  - Catalytic Domain/genetics/physiology
MH  - Cell Nucleus/enzymology
MH  - Cloning, Molecular
MH  - Cytoplasm/enzymology
MH  - Fibroblasts
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Peptide Fragments/chemistry/genetics/isolation & purification/metabolism
MH  - Poly(ADP-ribose) Polymerase Inhibitors
MH  - Poly(ADP-ribose) Polymerases/chemistry/genetics/*metabolism
MH  - RNA, Messenger/analysis/genetics
MH  - Sequence Homology, Amino Acid
MH  - Spindle Apparatus/enzymology
MH  - Vault Ribonucleoprotein Particles/chemistry/genetics/isolation &
      purification/metabolism
MH  - Yeasts/genetics
PMC - PMC2169495
EDAT- 1999/09/09 00:00
MHDA- 1999/09/09 00:01
CRDT- 1999/09/09 00:00
PHST- 1999/09/09 00:00 [pubmed]
PHST- 1999/09/09 00:01 [medline]
PHST- 1999/09/09 00:00 [entrez]
AID - 10.1083/jcb.146.5.917 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Sep 6;146(5):917-28. doi: 10.1083/jcb.146.5.917.