DNA-damage response in chromatin of ribosomal genes and the surrounding genome

Foltánková, Veronika; Legartová, Soňa; Kozubek, Stanislav; Höfer, Milan; Bártová, Eva

doi:10.1016/j.gene.2013.03.108

Cited by 21 publications

(28 citation statements)

References 43 publications

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“…Dellaire et al [] additionally showed simultaneous appearance of DSBs in parallel with an increased number of PML nuclear bodies (NBs). This observation was supported recently by Foltankova et al []. PML NBs also non‐randomly associate with γH2AX‐, Rad51‐, and RPA‐positive foci that are induced after γ‐irradiation.…”

supporting

confidence: 70%

“…Moreover, many DNA repair‐related proteins, such as ATR, MRE11, or NBS1 accumulate in close proximity to PML NBs after cell exposure to ionizing radiation [Lombard and Guarente, ; Bischof et al, ; Mirzoeva and Petrini, ; Barr et al, ]. Recently, we have observed an increasing co‐localization between PML bodies and 53BP1‐positive DNA lesions in γ‐irradiated cells [Foltankova et al, ]. Interestingly, movement of PML bodies co‐localizing with 53BP1 NBs was limited in irradiated cells as revealed by single particle tracking analysis [Foltankova et al, ].…”

mentioning

confidence: 94%

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Localized Movement and Levels of 53BP1 Protein Are Changed by γ‐irradiation in PML Deficient Cells

Legartová

Sehnalová

Malyšková

et al. 2016

J of Cellular Biochemistry

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We studied epigenetics, distribution pattern, kinetics, and diffusion of proteins recruited to spontaneous and γ-radiation-induced DNA lesions. We showed that PML deficiency leads to an increased number of DNA lesions, which was accompanied by changes in histone signature. In PML wt cells, we observed two mobile fractions of 53BP1 protein with distinct diffusion in spontaneous lesions. These protein fractions were not detected in PML-deficient cells, characterized by slow-diffusion of 53BP1. Single particle tracking analysis revealed limited local motion of 53BP1 foci in PML double null cells and local motion 53BP1 foci was even more reduced after γ-irradiation. However, radiation did not change co-localization between 53BP1 nuclear bodies and interchromatin granule-associated zones (IGAZs), nuclear speckles, or chromocenters. This newly observed interaction pattern imply that 53BP1 protein could be a part of not only DNA repair, but also process mediated via components accumulated in IGAZs, nuclear speckles, or paraspeckles. Together, PML deficiency affected local motion of 53BP1 nuclear bodies and changed composition and a number of irradiation-induced foci. J. Cell. Biochem. 117: 2583-2596, 2016. © 2016 Wiley Periodicals, Inc.

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confidence: 70%

mentioning

confidence: 94%

Localized Movement and Levels of 53BP1 Protein Are Changed by γ‐irradiation in PML Deficient Cells

Legartová

Sehnalová

Malyšková

et al. 2016

J of Cellular Biochemistry

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“…However, the DDR-related function of proteins such as coilin, which can appear in nucleoli of tumor cells, is less understood. 14,[25][26][27] Recently, it was observed that nucleolar accumulation of coilin was influenced by both cisplatin and γ-radiation, which induced co-localization of coilin and the RNA Pol I subunit RPA194. Radiation also enhances the interaction between coilin and UBF factors that modulate the association of RNA Pol I with rDNA.…”

Section: Discussionmentioning

confidence: 99%

Coilin is rapidly recruited to UVA-induced DNA lesions and γ-radiation affects localized movement of Cajal bodies

Bártová

Foltánková

Legartová

et al. 2014

Nucleus

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“…The concept of histone-depleted active rRNA genes was challenged by findings using chromatin immunoprecipitation (ChIP), which led to the conclusion that significant amounts of histones are present on active rRNA genes not impeding Pol I transcription in yeast (Jones et al 2007) and in mammalian cells (Foltankova et al 2013). Interestingly, in protozoa, it was recently reported that nucleosomal organization exists within the coding region and the IGS, whereas the promoter is free of histones (Vizuet-de-Rueda et al 2016), which might point to evolutionary differences in nucleolar chromatin organization.…”

Section: Nucleolar Morphology and Regulation Of Gene Transcriptionmentioning

confidence: 99%

Nucleolus and chromatin

Schöfer

Weipoltshammer

2018

Histochem Cell Biol

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The nucleolus as site of ribosome biogenesis holds a pivotal role in cell metabolism. It is composed of ribosomal DNA (rDNA), which is present as tandem arrays located in nucleolus organizer regions (NORs). In interphase cells, rDNA can be found inside and adjacent to nucleoli and the location is indicative for transcriptional activity of ribosomal genes—inactive rDNA (outside) versus active one (inside). Moreover, the nucleolus itself acts as a spatial organizer of non-nucleolar chromatin. Microscopy-based approaches offer the possibility to explore the spatially distinct localization of the different DNA populations in relation to the nucleolar structure. Recent technical developments in microscopy and preparatory methods may further our understanding of the functional architecture of nucleoli. This review will attempt to summarize the current understanding of mammalian nucleolar chromatin organization as seen from a microscopist’s perspective.

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DNA-damage response in chromatin of ribosomal genes and the surrounding genome

Cited by 21 publications

References 43 publications

Localized Movement and Levels of 53BP1 Protein Are Changed by γ‐irradiation in PML Deficient Cells

Localized Movement and Levels of 53BP1 Protein Are Changed by γ‐irradiation in PML Deficient Cells

Coilin is rapidly recruited to UVA-induced DNA lesions and γ-radiation affects localized movement of Cajal bodies

Nucleolus and chromatin

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