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Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence
T Kurosaki1, H Ushiro, Y Mitsuuchi
1Department of Medical Chemistry, Kochi Medical School, Japan.
The Journal of Biological Chemistry
|November 25, 1987
Summary
Researchers sequenced human poly(ADP-ribose) synthetase cDNA, revealing a 1,013-amino acid protein. The DNA-binding domain shows homology to oncogenes, suggesting a role in eukaryotic cell transformation control.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Human poly(ADP-ribose) synthetase has distinct DNA-binding, automodification, and NAD-binding domains.
- Understanding the enzyme's structure and function is crucial for cellular processes.
Purpose of the Study:
- To isolate and sequence cDNA clones for human poly(ADP-ribose) synthetase.
- To elucidate the protein's primary structure and potential functional domains.
Main Methods:
- Isolation and sequencing of cDNA clones using synthesized oligodeoxyribonucleotide probes.
- Deduction of amino acid sequence from cDNA.
- Analysis of hydrophilicity and charge distribution.
Main Results:
- A cDNA open reading frame encoding a 1,013-amino acid protein (113,203 Da) was identified.
- The deduced amino acid sequence aligns with experimental peptide data and amino acid composition.
- The DNA-binding domain exhibits homology to oncogenic proteins (c-fos, v-fos) and contains nuclear localization signals.
Conclusions:
- The DNA-binding domain's homology to oncogenes and nuclear localization signals suggests a role in DNA binding and eukaryotic cell transformation.
- Poly(ADP-ribose) synthetase may function in controlling cell transformation, similar to oncogene products.