An Alternative Form of Poly(ADP-Ribose) Polymerase inDrosophila melanogasterand Its Ectopic Expression in Rat-1 Cells

• Published in: Biochemical and biophysical research communications Vol. 251; no. 1; pp. 35 - 40
• Main Authors: Kawamura, Tomonori, Hanai, Shuji, Yokota, Tomoko, Hayashi, Takashi, Poltronieri, Palmiro, Miwa, Masanao, Uchida, Kazuhiko
• Format: Journal Article
• Language: English; Japanese
• Published: Elsevier Inc 01.10.1998
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1998.9403

We here report an alternatively spliced form of PARP lacking exon 5 of theDrosophilaPARP 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-lengthDrosophila PARPcDNA, 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.