Number of the records: 1  

G-Quadruplex Structures Colocalize with Transcription Factories and Nuclear Speckles Surrounded by Acetylated and Dimethylated Histones H3

  1. 1.
    0541561 - BFÚ 2022 RIV CH eng J - Journal Article
    Komůrková, Denisa - Svobodová Kovaříková, Alena - Bártová, Eva
    G-Quadruplex Structures Colocalize with Transcription Factories and Nuclear Speckles Surrounded by Acetylated and Dimethylated Histones H3.
    International Journal of Molecular Sciences. Roč. 22, č. 4 (2021), č. článku 1995. E-ISSN 1422-0067
    R&D Projects: GA ČR(CZ) GA18-07384S
    Institutional support: RVO:68081707
    Keywords : G-quadruplex structure * epigenetics * nuclear bodies * transcription factories * nuclear speckles * DNA repair
    OECD category: Biochemistry and molecular biology
    Impact factor: 6.208, year: 2021
    Method of publishing: Open access
    https://www.mdpi.com/1422-0067/22/4/1995

    G-quadruplexes (G4s) are four-stranded helical structures that regulate several nuclear processes, including gene expression and telomere maintenance. We observed that G4s are located in GC-rich (euchromatin) regions and outside the fibrillarin-positive compartment of nucleoli. Genomic regions around G4s were preferentially H3K9 acetylated and H3K9 dimethylated, but H3K9me3 rarely decorated G4 structures. We additionally observed the variability in the number of G4s in selected human and mouse cell lines. We found the highest number of G4s in human embryonic stem cells. We observed the highest degree of colocalization between G4s and transcription factories, positive on the phosphorylated form of RNA polymerase II (RNAP II). Similarly, a high colocalization rate was between G4s and nuclear speckles, enriched in pre-mRNA splicing factor SC-35. PML bodies, the replication protein SMD1, and Cajal bodies colocalized with G4s to a lesser extent. Thus, G4 structures seem to appear mainly in nuclear compartments transcribed via RNAP II, and pre-mRNA is spliced via the SC-35 protein. However, alpha-amanitin, an inhibitor of RNAP II, did not affect colocalization between G4s and transcription factories as well as G4s and SC-35-positive domains. In addition, irradiation by gamma-rays did not change a mutual link between G4s and DNA repair proteins (G4s/gamma H2AX, G4s/53BP1, and G4s/MDC1), accumulated into DNA damage foci. Described characteristics of G4s seem to be the manifestation of pronounced G4s stability that is likely maintained not only via a high-order organization of these structures but also by a specific histone signature, including H3K9me2, responsible for chromatin compaction.
    Permanent Link: http://hdl.handle.net/11104/0319103

     
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.