skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase

Abstract

Recently the authors described a full-length cDNA for the human nuclear enzyme poly(ADP-ribose) polymerase. Here, they report the chromosomal localization and partial map of the human gene for this enzyme as well as the complete coding sequence for this protein. The nucleotide sequence reveals a single 3042-base open reading frame encoding a protein with a predicted M/sub r/ of 113,135. A comparison of this deduced amino acid sequence with the amino acid sequence of three peptides derived from human poly(ADP-ribose) polymerase revealed a match of 27 amino acid residues. A computer-derived structural analysis of the enzyme and a search for similarities with other proteins confirmed that the polymerase belongs to a subfamily of DNA/NAD-binding proteins and DNA-repair proteins. Possible Zn/sup 2 +/-binding fingers, a nucleotide-binding fold, and a nuclear transport signal were noted. Additionally, chromosomal mapping has identified polymerase-hybridizing sequences on human chromosomes 1 (the active gene), 13, and 14 (processed pseudogenes). Using the polymerase cDNA as a probe, they also have detected several DNA restriction fragment length polymorphisms in normal humans.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Georgetown Univ. Schools of Medicine and Dentistry, Washington, DC (USA)
OSTI Identifier:
6468240
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. U.S.A.; (United States)
Additional Journal Information:
Journal Volume: 84:23
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GENES; DNA SEQUENCING; GENETIC MAPPING; POLYMERASES; AMINO ACID SEQUENCE; CATIONS; HETEROCHROMOSOMES; HYBRIDIZATION; MAN; PHOSPHORUS 32; RFLPS; ZINC COMPOUNDS; ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CHARGED PARTICLES; CHROMOSOMES; DAYS LIVING RADIOISOTOPES; ENZYMES; IONS; ISOTOPES; LIGHT NUCLEI; MAMMALS; MAPPING; MOLECULAR STRUCTURE; NUCLEI; NUCLEOTIDYLTRANSFERASES; ODD-ODD NUCLEI; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; PRIMATES; RADIOISOTOPES; STRUCTURAL CHEMICAL ANALYSIS; TRANSFERASES; VERTEBRATES; 550401* - Genetics- Tracer Techniques

Citation Formats

Cherney, B W, McBride, O W, Chen, D, Alkhatib, H, Bhatia, K, Hensley, P, and Smulson, M E. cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. United States: N. p., 1987. Web. doi:10.1073/pnas.84.23.8370.
Cherney, B W, McBride, O W, Chen, D, Alkhatib, H, Bhatia, K, Hensley, P, & Smulson, M E. cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. United States. https://doi.org/10.1073/pnas.84.23.8370
Cherney, B W, McBride, O W, Chen, D, Alkhatib, H, Bhatia, K, Hensley, P, and Smulson, M E. 1987. "cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase". United States. https://doi.org/10.1073/pnas.84.23.8370.
@article{osti_6468240,
title = {cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase},
author = {Cherney, B W and McBride, O W and Chen, D and Alkhatib, H and Bhatia, K and Hensley, P and Smulson, M E},
abstractNote = {Recently the authors described a full-length cDNA for the human nuclear enzyme poly(ADP-ribose) polymerase. Here, they report the chromosomal localization and partial map of the human gene for this enzyme as well as the complete coding sequence for this protein. The nucleotide sequence reveals a single 3042-base open reading frame encoding a protein with a predicted M/sub r/ of 113,135. A comparison of this deduced amino acid sequence with the amino acid sequence of three peptides derived from human poly(ADP-ribose) polymerase revealed a match of 27 amino acid residues. A computer-derived structural analysis of the enzyme and a search for similarities with other proteins confirmed that the polymerase belongs to a subfamily of DNA/NAD-binding proteins and DNA-repair proteins. Possible Zn/sup 2 +/-binding fingers, a nucleotide-binding fold, and a nuclear transport signal were noted. Additionally, chromosomal mapping has identified polymerase-hybridizing sequences on human chromosomes 1 (the active gene), 13, and 14 (processed pseudogenes). Using the polymerase cDNA as a probe, they also have detected several DNA restriction fragment length polymorphisms in normal humans.},
doi = {10.1073/pnas.84.23.8370},
url = {https://www.osti.gov/biblio/6468240}, journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 84:23,
place = {United States},
year = {Tue Dec 01 00:00:00 EST 1987},
month = {Tue Dec 01 00:00:00 EST 1987}
}