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Genomics. 1999 May 1;57(3):442-5.

A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues.

Author information

  • Division of Clinical Virology F68, Huddinge University Hospital, Stockholm, S-141 86, Sweden. magnus.johansson@mbb.ki.se

Abstract

Posttranscriptional modification of nuclear proteins by poly(ADP-ribosyl)ation in response to DNA strand breaks plays an important role in DNA repair, regulation of apoptosis, and maintenance of genomic stability. A 113-kDa human poly(ADP-ribose) polymerase (PARP) has previously been identified and cloned. However, there is evidence that additional enzymes with PARP activity exist in mammalian cells. I have identified and cloned the cDNAs of two novel approximately 60-kDa human proteins that are 40 and 31% identical to the catalytic C-terminal domain of PARP. These proteins, named PARP-2 and PARP-3, lack the DNA-binding and automodification domains. PARP-2 and PARP-3 mRNAs were detected in 16 different human tissues as major bands of 2.0 and 2.2 kb, respectively. Radiation hybrid analysis assigned the PARP-2 gene (HGMW-approved symbol ADPRTL2) to chromosome 14q11.2-q12 and the PARP-3 gene (HGMW-approved symbol ADPRTL3) to 3p21.1-p22.2. This report shows the existence of a human PARP gene family with at least three closely related members.

Copyright 1999 Academic Press.

PMID:
10329013
[PubMed - indexed for MEDLINE]
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