Biochem. J. (2002) 368
(263–271) (Printed in Great Britain)
The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in Caenorhabditis elegans
Steve N. GAGNON* , Michael O. HENGARTNER† and Serge DESNOYERS*1
*Department of Pediatrics, Laval University Medical Research Centre and Faculty of Medicine, Laval University, Quebec, Canada, and †Institute of Molecular Biology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
Poly(ADP-ribose) polymerases (PARPs) are an expanding, well-conserved family of enzymes found in many metazoan species, including plants. The enzyme catalyses poly(ADP-ribosyl)ation, a post-translational modification that is important in DNA repair and programmed cell death. In the present study, we report the finding of an endogenous source of poly(ADP-ribosyl)ation in total extracts of the nematode Caenorhabditis elegans. Two cDNAs encoding highly similar proteins to human PARP-1 (huPARP-1) and huPARP-2 are described, and we propose to name the corresponding enzymes poly(ADP-ribose) metabolism enzyme 1 (PME-1) and PME-2 respectively. PME-1 (108kDa) shares 31% identity with huPARP-1 and has an overall structure similar to other PARP-1 subfamily members. It contains sequences having considerable similarity to zinc-finger motifs I and II, as well as with the catalytic domain of huPARP-1. PME-2 (61kDa) has structural similarities with the catalytic domain of PARPs in general and shares 24% identity with huPARP-2. Recombinant PME-1 and PME-2 display PARP activity, which may partially account for the similar activity found in the worm. A partial duplication of the pme-1 gene with pseudogene-like features was found in the nematode genome. Messenger RNA for pme-1 are 5´-tagged with splice leader 1, whereas those for pme-2 are tagged with splice leader 2, suggesting an operon-like expression for pme-2. The expression pattern of pme-1 and pme-2 is also developmentally regulated. Together, these results show that PARP-1 and -2 are conserved in evolution and must have important functions in multicellular organisms. We propose using C. elegans as a model to understand better the functions of these enzymes.
Key words: development, gene expression, post-translational modification, worm.
Abbreviations used: IPTG, isopropyl b-D-thiogalactoside; ORF, open reading frame; PARG, poly(ADP-ribose) glycohydrolase; PARP, poly(ADP-ribose) polymerase; huPARP, human PARP; PME-1, poly(ADP-ribose) metabolism enzyme 1; RT, reverse transcriptase; SL, splice leader; UTR, untranslated region; ZF, zinc finger.
1To whom correspondence should be addressed (e-mail serge.desnoyers@crchul.ulaval.ca).
The nucleotide sequence data for pme-1 and pme-2 have been submitted to the GenBank® Nucleotide Sequence Database under the accession numbers AF499444 and AF500111 respectively.
Received 26 April 2002/26 July 2002; accepted 29 July 2002
Published as BJ Immediate Publication 29 July 2002, DOI 10.1042/BJ20020669
The Biochemical Society, London ©
2002
*Unofficial Impact Factors
Unofficial 2010 Impact Factor for BJ Disease calculated by dividing the number of times articles published in 2008 and 2009 were cited in 2010 (based on a search of the Web of ScienceSM Thomson Reuters) by the number of articles published in 2008 and 2009.
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