scholarly journals Cockayne syndrome group B protein promotes mitochondrial DNA stability by supporting the DNA repair association with the mitochondrial membrane

2010 ◽  
Vol 24 (7) ◽  
pp. 2334-2346 ◽  
Author(s):  
Maria D. Aamann ◽  
Martin M. Sorensen ◽  
Christina Hvitby ◽  
Brian R. Berquist ◽  
Meltem Muftuoglu ◽  
...  
Keyword(s):  
Dna Repair ◽  
Mitochondrial Dna ◽  
Mitochondrial Membrane ◽  
Cockayne Syndrome ◽  
Dna Stability ◽  
Group B ◽  
Mitochondrial Dna Stability

The Cockayne syndrome group B DNA repair protein as an anti-cancer target

2001 ◽  
Author(s):  
Y. Lu ◽  
Sridhar Mani ◽  
Ekambar Kandimalla ◽  
Dong Yu ◽  
Sudhir Agrawal ◽  
...  
Keyword(s):  
Dna Repair ◽  
Cockayne Syndrome ◽  
Repair Protein ◽  
Anti Cancer ◽  
Dna Repair Protein ◽  
Group B

scholarly journals Cardiolipin Is Not Required to Maintain Mitochondrial DNA Stability or Cell Viability forSaccharomyces cerevisiaeGrown at Elevated Temperatures

2003 ◽  
Vol 278 (37) ◽  
pp. 35204-35210 ◽  
Author(s):  
Mei Zhang ◽  
Xuefeng Su ◽  
Eugenia Mileykovskaya ◽  
Andrew A. Amoscato ◽  
William Dowhan
Keyword(s):  
Mitochondrial Dna ◽  
Cell Viability ◽  
Elevated Temperatures ◽  
Dna Stability ◽  
Mitochondrial Dna Stability

scholarly journals Poly(ADP-ribose) polymerase 1 (PARP1) promotes oxidative stress–induced association of Cockayne syndrome group B protein with chromatin

2018 ◽  
Vol 293 (46) ◽  
pp. 17863-17874 ◽  
Author(s):  
Erica L. Boetefuer ◽  
Robert J. Lake ◽  
Kostiantyn Dreval ◽  
Hua-Ying Fan
Keyword(s):  
Oxidative Stress ◽  
Dna Repair ◽  
Rna Polymerase Ii ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Transcription Elongation ◽  
Cockayne Syndrome ◽  
Base Excision ◽  
Group B ◽  
Genomic Regions

Cockayne syndrome protein B (CSB) is an ATP-dependent chromatin remodeler that relieves oxidative stress by regulating DNA repair and transcription. CSB is proposed to participate in base-excision repair (BER), the primary pathway for repairing oxidative DNA damage, but exactly how CSB participates in this process is unknown. It is also unclear whether CSB contributes to other repair pathways during oxidative stress. Here, using a patient-derived CS1AN-sv cell line, we examined how CSB is targeted to chromatin in response to menadione-induced oxidative stress, both globally and locus-specifically. We found that menadione-induced, global CSB–chromatin association does not require CSB's ATPase activity and is, therefore, mechanistically distinct from UV-induced CSB–chromatin association. Importantly, poly(ADP-ribose) polymerase 1 (PARP1) enhanced the kinetics of global menadione-induced CSB–chromatin association. We found that the major BER enzymes, 8-oxoguanine DNA glycosylase (OGG1) and apurinic/apyrimidinic endodeoxyribonuclease 1 (APE1), do not influence this association. Additionally, the level of γ-H2A histone family member X (γ-H2AX), a marker for dsDNA breaks, was not increased in menadione-treated cells. Therefore, our results support a model whereby PARP1 localizes to ssDNA breaks and recruits CSB to participate in DNA repair. Furthermore, this global CSB–chromatin association occurred independently of RNA polymerase II–mediated transcription elongation. However, unlike global CSB–chromatin association, both PARP1 knockdown and inhibition of transcription elongation interfered with menadione-induced CSB recruitment to specific genomic regions. This observation supports the hypothesis that CSB is also targeted to specific genomic loci to participate in transcriptional regulation in response to oxidative stress.

scholarly journals Aspartate β-hydroxylase disrupts mitochondrial DNA stability and function in hepatocellular carcinoma

Oncogenesis ◽  
2017 ◽  
Vol 6 (7) ◽  
pp. e362-e362 ◽  
Author(s):  
C Tang ◽  
Y Hou ◽  
H Wang ◽  
K Wang ◽  
H Xiang ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Mitochondrial Dna ◽  
Dna Stability ◽  
And Function ◽  
Mitochondrial Dna Stability
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