DNA Damage-Induced Transcriptional Activation of a Human DNA Polymerase .beta. Chimeric Promoter: Recruitment of Preinitiation Complex in Vitro by ATF/CREB

Biochemistry ◽  
1995 ◽  
Vol 34 (1) ◽  
pp. 73-80 ◽  
Author(s):  
Satya Narayan ◽  
William A. Beard ◽  
Samuel H. Wilson
Keyword(s):  
Dna Damage ◽  
Dna Polymerase ◽  
Transcriptional Activation ◽  
Dna Polymerase Beta ◽  
Preinitiation Complex ◽  
Chimeric Promoter ◽  
Polymerase Beta ◽  
Human Dna ◽  
Promoter Recruitment

scholarly journals Involvement of deoxyribonucleic acid polymerase β in nuclear deoxyribonucleic acid synthesis

1978 ◽  
Vol 173 (1) ◽  
pp. 309-314 ◽  
Author(s):  
T R Butt ◽  
W M Wood ◽  
E L McKay ◽  
R L P Adams
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Deoxyribonucleic Acid ◽  
Nuclear Dna ◽  
Dna Polymerase Beta ◽  
Cell Nuclei ◽  
High Molecular Weight Dna ◽  
Dna Polymerase Alpha ◽  
Polymerase Beta

The effects on DNA synthesis in vitro in mouse L929-cell nuclei of differential extraction of DNA polymerases alpha and beta were studied. Removal of all measurable DNA polymerase alpha and 20% of DNA polymerase beta leads to a 40% fall in the replicative DNA synthesis. Removal of 70% of DNA polymerase beta inhibits replicative synthesis by 80%. In all cases the nuclear DNA synthesis is sensitive to N-ethylmaleimide and aCTP (arabinosylcytosine triphosphate), though less so than DNA polymerase alpha. Addition of deoxyribonuclease I to the nuclear incubation leads to synthesis of high-molecular-weight DNA in a repair reaction. This occurs equally in nuclei from non-growing or S-phase cells. The former nuclei lack DNA polymerase alpha and the reaction reflects the sensitivity of DNA polymerase beta to inhibiton by N-ethylmaleimide and aCTP.

scholarly journals DNA polymerase beta bypasses in vitro a single d(GpG)-cisplatin adduct placed on codon 13 of the HRAS gene.

1995 ◽  
Vol 92 (12) ◽  
pp. 5356-5360 ◽  
Author(s):  
J. S. Hoffmann ◽  
M. J. Pillaire ◽  
G. Maga ◽  
V. Podust ◽  
U. Hubscher ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Beta ◽  
Polymerase Beta ◽  
Hras Gene

scholarly journals Inactivation of DNA polymerase beta by in vitro phosphorylation with protein kinase C

1991 ◽  
Vol 266 (17) ◽  
pp. 10820-10824
Author(s):  
T. Tokui ◽  
M. Inagaki ◽  
K. Nishizawa ◽  
R. Yatani ◽  
M. Kusagawa ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Polymerase ◽  
Dna Polymerase Beta ◽  
Polymerase Beta ◽  
Kinase C

Expression of human DNA polymerase .beta. in Escherichia coli and characterization of the recombinant enzyme

Biochemistry ◽  
1988 ◽  
Vol 27 (3) ◽  
pp. 901-909 ◽  
Author(s):  
John Abbotts ◽  
Dibyendu N. SenGupta ◽  
Barbara Zmudzka ◽  
Steven G. Widen ◽  
Vicente Notario ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Recombinant Enzyme ◽  
Dna Polymerase Beta ◽  
Polymerase Beta ◽  
Human Dna

MDM2 Dependant Induction of Error Prone DNA Polymerase beta by EBV-LMP1 Oncoprotein.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 3008-3008
Author(s):  
Faumont Nathalie ◽  
Le Clorennec Christophe ◽  
Teira Pierre ◽  
Youlyouz-Marfak Ibtissam ◽  
Mazeres Christine ◽  
...  
Keyword(s):  
Protein Expression ◽  
Dna Polymerase ◽  
Dna Polymerase Beta ◽  
Tumour Necrosis Factor Receptor ◽  
Regulatory Sequences ◽  
Mdm2 Protein ◽  
Polymerase Beta ◽  
Human Tumours ◽  
Nf Kappab

Abstract Epstein Barr Virus (EBV) is able to immortalise B lymphocytes in vitro and is associated with several human tumours, such as Hodgkin’s disease (HD), suggesting that this virus could play a role in the initiation of the tumoural process. The LMP1 protein of EBV, coded by the LMP1-BNLF1 gene, was rapidly suspected to be involved in this process due to its oncogenic characteristics. LMP1 functions as a constitutively activated member of the tumour necrosis factor receptor superfamily, and activates trough its carboxyterminal cytoplasmic region several signalling pathways, including NF-kappa B. In order to identify new LMP1 target genes, we studied the transcriptome of the B lymphoid Ba/F3 cell line stably transfected with LMP1-BNLF1 genes from HD Reed-Sternberg tumour cells as well as from normal cells, using the cDNA microarray technique. We show that the expression of several genes was modulated by the LMP1 protein, independently of the cellular origin of the LMP1 protein. Among overexpressed genes, we focused on the DNA polymerase-beta (beta-pol) gene. To confirm and extend this cDNA result, we demonstrated in different cell lines that the beta-pol protein expression was under the control of LMP1. In vivo and in vitro functional tests showed that LMP1 induced overexpression of beta-pol paralleled its increase in activity. Regulatory sequences of the human beta-pol gene includes three motives that match the Sp1 factor binding site motive. LMP1 did not modulate Sp1 RNA neither protein expression. By contrast, we observed that MDM2 and beta-pol RNA expression were increased in parallel by LMP1, an effect trigerred by the carboxyterminal region of LMP1. Then, we demonstrated that MDM2 protein overexpression was associated with increased beta-pol protein expression. Since MDM2 promoter is regulated by NF-kappaB, we investigated whether up-regulation of MDM2 and beta-pol were NF-kappaB pathway dependant. We show that inhibition of NF-kappaB by overexpression of an I-kappaB dominant negative down-regulated both MDM2 and beta-pol expression. In conclusion, we demonstrated that the oncoprotein LMP1 regulates overexpression of beta-pol through NF-kappaB signaling pathway and the MDM2 protein, and that MDM2 was itself regulated by NF-kappaB. Beta-pol is the more error prone of all the known eucaryotic DNA polymerases. Elevated expression of beta-pol, an event found in many human tumours, has been shown to generate a mutator phenotype which is extensively associated with cancers. Our work leads to the hypothesis that LMP1 protein could play a role in the genetic instability in EBV associated malignant diseases such as HD through over-expression of beta-pol.

scholarly journals Characterization of Messenger RNA for Chick-Embryo DNA Polymerase beta and Its Translation Product in vitro

1983 ◽  
Vol 133 (2) ◽  
pp. 277-282 ◽  
Author(s):  
Masamitsu YAMAGUCHI ◽  
Taijo TAKAHASHI ◽  
Kunio YASUDA ◽  
Yoshiro SHIMURA ◽  
Akio MATSUKAGE
Keyword(s):  
Chick Embryo ◽  
Dna Polymerase ◽  
Messenger Rna ◽  
Dna Polymerase Beta ◽  
Translation Product ◽  
Polymerase Beta
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