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Pregled bibliografske jedinice broj: 1006497

Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity


Akoury, Elias; Ma, Guoli; Demolin, Segolene; Brönner, Cornelia; Zocco, Manuel; Cirilo, Alexandre; Ivić, Nives; Halić, Mario
Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity // Nucleic acids research, 47 (2019), 13; 6726-6736 doi:10.1093/nar/gkz480 (međunarodna recenzija, članak, znanstveni)


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Naslov
Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity

Autori
Akoury, Elias ; Ma, Guoli ; Demolin, Segolene ; Brönner, Cornelia ; Zocco, Manuel ; Cirilo, Alexandre ; Ivić, Nives ; Halić, Mario

Izvornik
Nucleic acids research (0305-1048) 47 (2019), 13; 6726-6736

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
nucleosome ; H3K9 methylation ; heterochromatin ; H3K9 methyltransferase ; RNA

Sažetak
Heterochromatin is a distinctive chromatin structure that is essential for chromosome segregation, genome stability and regulation of gene expression. H3K9 methylation (H3K9me), a hallmark of heterochromatin, is deposited by the Su(var)3-9 family of proteins ; however, the mechanism by which H3K9 methyltransferases bind and methylate the nucleosome is poorly understood. In this work we determined the interaction of Clr4, the fission yeast H3K9 methyltransferase, with nucleosomes using nuclear magnetic resonance, biochemical and genetic assays. Our study shows that the Clr4 chromodomain binds the H3K9me3 tail and that both, the chromodomain and the disordered region connecting the chromodomain and the SET domain, bind the nucleosome core. We show that interaction of the disordered region with the nucleosome core is independent of H3K9me and contributes to H3K9me in vitro and in vivo. Moreover, we show that those interactions with the nucleosome core are contributing to de novo deposition of H3K9me and to establishment of heterochromatin.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Ustanove:
Institut "Ruđer Bošković", Zagreb

Profili:

Avatar Url Nives Ivić (autor)

Poveznice na cjeloviti tekst rada:

doi academic.oup.com www.ncbi.nlm.nih.gov doi.org

Citiraj ovu publikaciju:

Akoury, Elias; Ma, Guoli; Demolin, Segolene; Brönner, Cornelia; Zocco, Manuel; Cirilo, Alexandre; Ivić, Nives; Halić, Mario
Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity // Nucleic acids research, 47 (2019), 13; 6726-6736 doi:10.1093/nar/gkz480 (međunarodna recenzija, članak, znanstveni)
Akoury, E., Ma, G., Demolin, S., Brönner, C., Zocco, M., Cirilo, A., Ivić, N. & Halić, M. (2019) Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. Nucleic acids research, 47 (13), 6726-6736 doi:10.1093/nar/gkz480.
@article{article, year = {2019}, pages = {6726-6736}, DOI = {10.1093/nar/gkz480}, keywords = {nucleosome, H3K9 methylation, heterochromatin, H3K9 methyltransferase, RNA}, journal = {Nucleic acids research}, doi = {10.1093/nar/gkz480}, volume = {47}, number = {13}, issn = {0305-1048}, title = {Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity}, keyword = {nucleosome, H3K9 methylation, heterochromatin, H3K9 methyltransferase, RNA} }
@article{article, year = {2019}, pages = {6726-6736}, DOI = {10.1093/nar/gkz480}, keywords = {nucleosome, H3K9 methylation, heterochromatin, H3K9 methyltransferase, RNA}, journal = {Nucleic acids research}, doi = {10.1093/nar/gkz480}, volume = {47}, number = {13}, issn = {0305-1048}, title = {Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity}, keyword = {nucleosome, H3K9 methylation, heterochromatin, H3K9 methyltransferase, RNA} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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