TY - JOUR
T1 - DNA polymerase alpha from the nuclear matrix of cells infected with simian virus 40
AU - Jones, Clint
AU - Su, Robert T.
N1 - Funding Information:
ACKNOWLEDGMENTS We thank Drs. H. Sze, W. Haldenwang, J. Akagi, and D. Paretsky for the comments on the manuscript. This work was supported in part by General Research Funds from the University of Kansas and small grants from Mid-America Cancer Center to R.T.S. C. J. is a predoctoral fellow.
PY - 1982/9/25
Y1 - 1982/9/25
N2 - The nuclear matrix prepared from normal, simian virus 40 (SV40)-infected, and SV40-transformed cells contained DNA polymerase activities. Approximately 12% of the total DNA polymerase activities in isolated nuclei remained with the nuclear matrix, α-polymerase was the major matrix DNA polymerase activity as judged by sensitivity to various inhibitors: aphidicolin, dideoxy-TTP, and N-ethylmaleimide. Approximately 2-4 fold higher DNA polymerase activity was detected in matrices obtained from lytically infected and virus-transformed cells than that found in normal cells. In lytically infected cells, 30-50% of the matrix-bound DNA polymerase activity solubilized by sonication co-sedimented with majority of the matrix T-antigen, and was co-precipitated with anti-T sera. The results suggest that α-polymerase and viral T-antigen may form a functional complex in the matrix.
AB - The nuclear matrix prepared from normal, simian virus 40 (SV40)-infected, and SV40-transformed cells contained DNA polymerase activities. Approximately 12% of the total DNA polymerase activities in isolated nuclei remained with the nuclear matrix, α-polymerase was the major matrix DNA polymerase activity as judged by sensitivity to various inhibitors: aphidicolin, dideoxy-TTP, and N-ethylmaleimide. Approximately 2-4 fold higher DNA polymerase activity was detected in matrices obtained from lytically infected and virus-transformed cells than that found in normal cells. In lytically infected cells, 30-50% of the matrix-bound DNA polymerase activity solubilized by sonication co-sedimented with majority of the matrix T-antigen, and was co-precipitated with anti-T sera. The results suggest that α-polymerase and viral T-antigen may form a functional complex in the matrix.
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U2 - 10.1093/nar/10.18.5517
DO - 10.1093/nar/10.18.5517
M3 - Article
C2 - 6292844
AN - SCOPUS:0020491157
VL - 10
SP - 5517
EP - 5532
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 18
ER -