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Multivalency of nucleosome recognition by LEDGF

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00575033" target="_blank" >RIV/61388963:_____/23:00575033 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/23:00575033 RIV/00216224:14740/23:00133766 RIV/00216208:11310/23:10471752

  • Result on the web

    <a href="https://doi.org/10.1093/nar/gkad674" target="_blank" >https://doi.org/10.1093/nar/gkad674</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gkad674" target="_blank" >10.1093/nar/gkad674</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Multivalency of nucleosome recognition by LEDGF

  • Original language description

    Eukaryotic transcription is dependent on specific histone modifications. Their recognition by chromatin readers triggers complex processes relying on the coordinated association of transcription regulatory factors. Although various modification states of a particular histone residue often lead to differential outcomes, it is not entirely clear how they are discriminated. Moreover, the contribution of intrinsically disordered regions outside of the specialized reader domains to nucleosome binding remains unexplored. Here, we report the structures of a PWWP domain from transcriptional coactivator LEDGF in complex with the H3K36 di- and trimethylated nucleosome, indicating that both methylation marks are recognized by PWWP in a highly conserved manner. We identify a unique secondary interaction site for the PWWP domain at the interface between the acidic patch and nucleosomal DNA that might contribute to an H3K36-methylation independent role of LEDGF. We reveal DNA interacting motifs in the intrinsically disordered region of LEDGF that discriminate between the intra- or extranucleosomal DNA but remain dynamic in the context of dinucleosomes. The interplay between the LEDGF H3K36-methylation reader and protein binding module mediated by multivalent interactions of the intrinsically disordered linker with chromatin might help direct the elongation machinery to the vicinity of RNA polymerase II, thereby facilitating productive elongation.

  • 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

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

    1362-4962

  • Volume of the periodical

    51

  • Issue of the periodical within the volume

    18

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    10011-10025

  • UT code for WoS article

    001163598900001

  • EID of the result in the Scopus database

    2-s2.0-85175202376