Author Correction to: Telomerase subunit Est2 marks internal sites that are prone to accumulate DNA damage

An amendment to this paper has been published and can be accessed via the original article.</p

Telomerase subunit Est2 marks internal sites that are prone to accumulate DNA damage

BACKGROUND: The main function of telomerase is at the telomeres but under adverse conditions telomerase can bind to internal regions causing deleterious effects as observed in cancer cells. RESULTS: By mapping the global occupancy of the catalytic subunit of telomerase (Est2) in the budding yeast Saccharomyces cerevisiae, we reveal that it binds to multiple guanine-rich genomic loci, which we termed “non-telomeric binding sites” (NTBS). We characterize Est2 binding to NTBS. Contrary to telomeres, Est2 binds to NTBS in G1 and G2 phase independently of Est1 and Est3. The absence of Est1 and Est3 renders telomerase inactive at NTBS. However, upon global DNA damage, Est1 and Est3 join Est2 at NTBS and telomere addition can be observed indicating that Est2 occupancy marks NTBS regions as particular risks for genome stability. CONCLUSIONS: Our results provide a novel model of telomerase regulation in the cell cycle using internal regions as “parking spots” of Est2 but marking them as hotspots for telomere addition. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12915-021-01167-1

The effects of valproic acid on the mRNA expression of Natriuretic Peptide Receptor A and KQT-like subfamily Q-1 in human colon cancer cell lines

Aim and objectives: The histone deacetylase (HDAC) inhibitor, Valproic Acid (VPA), causes growth inhibition and apoptosis in colorectal cancer cells. HDAC inhibition is associated with the transcriptional regulation of Natriuretic Peptide Receptor-A (NPR-A). NPR-A regulates voltage-gated potassium channel, KQT-like subfamily Q, member 1 (KCNQ1). NPR-A and KCNQ1 are also involved in the initiation and propagation of cancer cells. In this study, we investigated the simultaneous expressional changes of NPR-A and KCNQ1 among VPA-treated colon cancer cells. Materials and methods: Human colorectal cancer cells were cultured and treated with increasing concentrations of VPA at different time points. MTT viability test was conducted to evaluate the growth inhibition. Real Time RT-PCR was used to quantify differential mRNA expression of NPR-A and KCNQ1 genes. Two-way ANOVA and bonferroni post-tests were used to analyze data statistically. Results: We showed that VPA treatment inhibits the growth of SW-480 cells more efficiently compared to HT-29. NPR-A and KCNQ1 genes were significantly upregulated upon VPA treatment in both cell lines (P < 0.0001). Conclusion: The alteration of NPR-A and KCNQ1 genes were more ordered among SW-480 cancer cells. The expressional changes of KCNQ1 and NPR-A among VPA treated human colon cancer cells follow the same pattern in similar combinations. VPA could regulate the expression of KCNQ1 through altering the mRNA expression of NPR-A

Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair

Nucleic acids can fold into G-quadruplex (G4) structures that can fine-tune biological processes. Proteins are required to recognize G4 structures and coordinate their function. Here we identify Zuo1 as a novel G4-binding protein in vitro and in vivo. In vivo in the absence of Zuo1 fewer G4 structures form, cell growth slows and cells become UV sensitive. Subsequent experiments reveal that these cellular changes are due to reduced levels of G4 structures. Zuo1 function at G4 structures results in the recruitment of nucleotide excision repair (NER) factors, which has a positive effect on genome stability. Cells lacking functional NER, as well as Zuo1, accumulate G4 structures, which become accessible to translesion synthesis. Our results suggest a model in which Zuo1 supports NER function and regulates the choice of the DNA repair pathway nearby G4 structures

Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair

G4 structure-interacting proteins have been linked to DNA repair processes. Here the authors reveal that in yeast, Zuo1 associates with G4 structures and plays a role in repair pathway choice by promoting nucleotide excision repair and ultimately contributing to maintenance of genome stability

Additional file 9 of Telomerase subunit Est2 marks internal sites that are prone to accumulate DNA damage

Supplementary Table 4. List of yeast strains used in this study

Author Correction to: Telomerase subunit Est2 marks internal sites that are prone to accumulate DNA damage (BMC Biology, (2021), 19, 1, (247), 10.1186/s12915-021-01167-1)

An amendment to this paper has been published and can be accessed via the original article