The team recently published an important manuscript showing an interplay between the linker histone Hho1p and Arp4p (a constituent of three chromatin modifying complexes in yeast)

Int J Biochem Cell Biol.
2014 Dec 24;59C:182-192. doi: 10.1016/j.biocel.2014.12.006. [Epub ahead of print]

The linker histone in Saccharomyces cerevisiae interacts with actin-related protein 4 and both regulate chromatin structure and cellular morphology.
 

Georgieva M¹, Staneva D¹, Uzunova K¹, Efremov T¹, Balashev K², Harata M³, Miloshev G⁴.

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Abstract

Chromatin structure promotes important epigenetic mechanisms that regulate cellular fate by organizing, preserving and controlling the way by which the genetic information works. Our understanding of chromatin and its functions is sparse and not yet well defined. The uncertainty comes from the complexity of chromatin and is induced by the existence of a large number of nuclear proteins that influence it. The intricate interaction among all these structural and functional nuclear proteins has been under extensive study in the recent years. Here, we show that Saccharomyces cerevisiae linker histone physically interacts with Arp4p (actin-related protein 4) which is a key subunit of three chromatin modifying complexes - INO80, SWR1 and NuA4. A single - point mutation in the actin - fold domain of Arp4p together with the knock-out of the gene for the linker histone in S. cerevisiae severely abrogates cellular and nuclear morphology and leads to complete disorganizing of the higher levels of chromatin organization.

Copyright © 2014 Elsevier Ltd. All rights reserved.

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