Rxivist logo

H3K36 methylation and DNA-binding are critical for Ioc4 recruitment and Isw1b remodeller function

By Jian Li, Lena Bergmann, Kimberly M Webb, Madelaine M Gogol, Philipp Voigt, Yingfang Liu, Huanhuan Liang, Michaela M. Smolle

Posted 26 Feb 2021
bioRxiv DOI: 10.1101/2021.02.26.432832

The Isw1b chromatin-remodelling complex is specifically recruited to gene bodies to help retain pre-existing histones during transcription by RNA polymerase II. Recruitment is dependent on H3K36 methylation and the Isw1b subunit Ioc4, which contains an N-terminal PWWP domain. Here, we present the crystal structure of the Ioc4-PWWP domain including a detailed functional characterization of the domain on its own as well as in the context of full-length Ioc4 and the Isw1b remodeller. Ioc4-PWWP preferentially binds H3K36me3-containing nucleosomes. The ability of the PWWP domain to bind DNA is required for this interaction. It is also promoted by the unique insertion motif present in Ioc4-PWWP. The ability to bind H3K36me3 as well as DNA are also critical for full-length Ioc4 binding to nucleosomes in vitro as well as its recruitment to gene bodies in vivo. Furthermore, a fully functional Ioc4-PWWP domain is necessary for efficient remodelling by Isw1b and the maintenance of ordered chromatin in vivo, thereby preventing intragenic transcription initiation and the production of non-coding RNAs.

Download data

  • Downloaded 105 times
  • Download rankings, all-time:
    • Site-wide: 140,101
    • In biochemistry: 4,235
  • Year to date:
    • Site-wide: 53,987
  • Since beginning of last month:
    • Site-wide: 110,376

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide