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ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F18%3A10389704" target="_blank" >RIV/00216208:11310/18:10389704 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.7554/eLife.41497" target="_blank" >https://doi.org/10.7554/eLife.41497</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.7554/eLife.41497" target="_blank" >10.7554/eLife.41497</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

  • Original language description

    Methylation of histone H3 at lysine 36 (H3K36me), a widely-distributed chromatin mark, largely results from association of the lysine methyltransferase (KMT) SET-2 with RNA polymerase II (RNAPII), but most eukaryotes also have additional H3K36me KMTs that act independently of RNAPII. These include the orthologs of ASH1, which are conserved in animals, plants, and fungi but whose function and control are poorly understood. We found that Neurospora crassa has just two H3K36 KMTs, ASH1 and SET-2, and were able to explore the function and distribution of each enzyme independently. While H3K36me deposited by SET-2 marks active genes, inactive genes are modified by ASH1 and its activity is critical for their repression. ASH1-marked chromatin can be further modified by methylation of H3K27, and ASH1 catalytic activity modulates the accumulation of H3K27me2/3 both positively and negatively. These findings provide new insight into ASH1 function, H3K27me2/3 establishment, and repression in facultative heterochromatin.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    eLife

  • ISSN

    2050-084X

  • e-ISSN

  • Volume of the periodical

    7

  • Issue of the periodical within the volume

    November 2018

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    19

  • Pages from-to

  • UT code for WoS article

    000450980800001

  • EID of the result in the Scopus database

    2-s2.0-85057082750