An alternative form of poly(ADP-ribose) polymerase in Drosophila melanogaster and its ectopic expression in rat-1 cells.
We here report an alternatively spliced form of PARP lacking exon 5 of the Drosophila PARP gene encoding the auto-modification domain. The alternative form of PARP (PARP II) consists 804 amino acids with a molecular weight of 92.3 kDa. The deduced amino acid sequence of PARP II was completely matched to that of PARP I encoded by a full-length Drosophila PARP cDNA, except it lacks the region corresponding to the auto-modification domain. To examine the function of PARP II, stable transformants of Rat-1 cells in which PARP II was ectopically expressed by MMTV-LTR were isolated and characterized. After induction with dexamethasone, PARP II transformants showed slower growth and showed morphological changes with loss of spindled shape compared to cells transformed with the vector or PARP I. The PARP II-transformed cells incorporated propidium iodide after induction; however, Annexin V and TUNEL analysis indicated these changes were not due to apoptosis.
Kawamura
T
T
Institute of Basic Medical Sciences, University of Tsukuba, Ibaraki, Tsukuba, 305-8575, Japan.
Hanai
S
S
Yokota
T
T
Hayashi
T
T
Poltronieri
P
P
Miwa
M
M
Uchida
K
K
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000235:genetics; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000302:isolation & purification; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics*; D005347:Fibroblasts; D007527:Isoenzymes / Q000096:biosynthesis* / Q000235:genetics; D008969:Molecular Sequence Data; D011065:Poly(ADP-ribose) Polymerases / Q000096:biosynthesis* / Q000235:genetics; D051381:Rats; D014170:Transformation, Genetic
D018076:DNA, Complementary; D007527:Isoenzymes; D011065:Poly(ADP-ribose) Polymerases