Response of human DNA polymerase ι promoter to N-methyl-N′-nitro-N-nitrosoguanidine

Zhu, Hongyu; Fan, Yanfeng; Jiang, H.; Shen, Jing; Qi, Hongyan; Mei, Ru-Huan; Shao, Jimin

doi:10.1016/j.etap.2009.11.001

Cited by 10 publications

(7 citation statements)

References 56 publications

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“…It is known that, to perform the TLS function, Y-family DNA polymerase members Pol, Pol, and Rev1 locate to replication factories with proliferating cell nuclear antigen and other proteins associated with replication in the nucleus, whereas different Y family polymerases may pass diverse types of DNA damage with different competency (1, 2). We previously found that Pol is transcriptionally up-regulated by MNNG exposure in an Sp1-dependent manner (55). In the current study, we demonstrated that MNNG exposure can stimulate up-regulation of Pol through IRF1 transactivation.…”

Section: Discussionsupporting

confidence: 54%

Interferon Regulatory Factor 1 Transactivates Expression of Human DNA Polymerase η in Response to Carcinogen N-Methyl-N′-nitro-N-nitrosoguanidine

Zhu

Meng

et al. 2012

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 54%

Interferon Regulatory Factor 1 Transactivates Expression of Human DNA Polymerase η in Response to Carcinogen N-Methyl-N′-nitro-N-nitrosoguanidine

Zhu

Meng

et al. 2012

Journal of Biological Chemistry

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“…Interestingly, in higher eukaryotes the access of the eukaryotic translesion polymerases to DNA shows a higher degree of coordination through ubiquitination of PCNA and the translesion polymerases ( Chun and Jin, 2010 ), as well as formation of polymerase bridges through Rev1 ( Pustovalova et al, 2016 ; Sale, 2013 ). However, given that there are up to 15 DNA polymerases to coordinate in eukaryotes ( Plosky and Woodgate, 2004 ), the ubiquitination of PCNA and the interactions between the polymerases may not be sufficient to coordinate the specific recruitment of individual translesion polymerases, implying that in eukaryotes too, the translesion process may occur at least in part by a concentration-dependent mechanism, which is supported by studies showing that the intracellular levels of several human translesion polymerases (Pol η, Pol κ, and Pol ι) are increased upon DNA damage ( Zhu et al, 2010 ; Zhu et al, 2012 ; Tomicic et al, 2014 ).…”

Section: Discussionmentioning

confidence: 99%

Single-molecule studies contrast ordered DNA replication with stochastic translesion synthesis

Zhao

Gleave

Lamers

2017

eLife

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High fidelity replicative DNA polymerases are unable to synthesize past DNA adducts that result from diverse chemicals, reactive oxygen species or UV light. To bypass these replication blocks, cells utilize specialized translesion DNA polymerases that are intrinsically error prone and associated with mutagenesis, drug resistance, and cancer. How untimely access of translesion polymerases to DNA is prevented is poorly understood. Here we use co-localization single-molecule spectroscopy (CoSMoS) to follow the exchange of the E. coli replicative DNA polymerase Pol IIIcore with the translesion polymerases Pol II and Pol IV. We find that in contrast to the toolbelt model, the replicative and translesion polymerases do not form a stable complex on one clamp but alternate their binding. Furthermore, while the loading of clamp and Pol IIIcore is highly organized, the exchange with the translesion polymerases is stochastic and is not determined by lesion-recognition but instead a concentration-dependent competition between the polymerases.

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“…We found that the transcription factor Sp1, but not Oct-1, was critical for upregulation of POLI gene transcription, which is consistent with previous findings in human FL cells. (28) Although several Oct-1 binding sites were found in the POLI promoter, the binding affinity of Oct-1 to the promoter was much weaker compared with that of Sp1. The binding affinity of Sp1 to the POLI promoter was also much higher in cancerous esophageal tissues than that in normal tissues.…”

Section: Discussionmentioning

confidence: 99%

Overexpression of DNA polymerase iota (Polι) in esophageal squamous cell carcinoma

et al. 2012

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The present study investigated the transcriptional regulation of low-fidelity translesion DNA synthesis (TLS) polymerases in human esophageal carcinoma. Significantly higher mRNA expression of polymerase zeta (Polξ), RAD18, polymerase iota (Polι), and polymerase kappa (Polj) was found in esophageal carcinomas. The increased expression of Polι in tumor samples was further confirmed by immunohistochemistry. The promoter of POLI that encodes Polι was found to be hypomethylated, although the overexpression of this gene was unlikely to be associated with methylation in tumors. We further identified Sp1 and Oct-1 binding sites present in the POLI promoter. We observed that the binding affinity of Sp1 to the POLI promoter was significantly increased in cancerous tissues and that Sp1 activated POLI gene transcription in cultured cell lines. The present study demonstrates overexpression of the TLS genes in esophageal carcinoma and identifies a key role for Sp1 in upregulating POLI gene expression. (Cancer Sci 2012; 103: 1574-1579

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Response of human DNA polymerase ι promoter to N-methyl-N′-nitro-N-nitrosoguanidine

Cited by 10 publications

References 56 publications

Interferon Regulatory Factor 1 Transactivates Expression of Human DNA Polymerase η in Response to Carcinogen N-Methyl-N′-nitro-N-nitrosoguanidine

Interferon Regulatory Factor 1 Transactivates Expression of Human DNA Polymerase η in Response to Carcinogen N-Methyl-N′-nitro-N-nitrosoguanidine

Single-molecule studies contrast ordered DNA replication with stochastic translesion synthesis

Overexpression of DNA polymerase iota (Polι) in esophageal squamous cell carcinoma

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