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Structural analysis of poly(ADP-ribose)polymerase in higher and lower eukaryotes
European Journal of Biochemistry
|August 15, 1986
Summary
Poly(ADP-ribose) polymerase, crucial for DNA repair, is conserved in vertebrates, arthropods, and mollusks. This enzyme
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Poly(ADP-ribose) polymerase (PARP) plays a vital role in DNA repair and genomic stability.
- Understanding the evolutionary distribution and structural conservation of PARP is essential for comprehending its function across diverse organisms.
Purpose of the Study:
- To conduct a phylogenetic survey of poly(ADP-ribose) polymerase across various organisms.
- To determine the structural characteristics and evolutionary conservation of the enzyme's catalytic peptides.
Main Methods:
- Enzyme activity analysis using in situ renaturation after electrophoresis in denaturing conditions (activity gel).
- Immunological detection using antiserum against calf thymus poly(ADP-ribose) polymerase.
Main Results:
- Poly(ADP-ribose) polymerase activity and a catalytic peptide (Mr = 115,000-120,000) were detected in vertebrates, arthropods, and mollusks.
- The enzyme was absent in echinoderms, nematodes, platyhelminths, thallophytes (including yeast), and bacteria.
- Immunoreactive peptides were found in vertebrates but not in non-vertebrate organisms.
Conclusions:
- The structure of poly(ADP-ribose) polymerase is conserved down to mollusks.
- This conservation suggests a significant role for PARP in the DNA metabolism of multicellular organisms.
- The findings provide insights into the evolutionary history and functional importance of PARP.