TY - JOUR
T1 - The linker histone in Saccharomyces cerevisiae interacts with actin-related protein 4 and both regulate chromatin structure and cellular morphology
AU - Georgieva, Milena
AU - Staneva, Dessislava
AU - Uzunova, Katya
AU - Efremov, Toni
AU - Balashev, Konstantin
AU - Harata, Masahiko
AU - Miloshev, George
N1 - Funding Information:
This work was supported by the Bulgarian Science Fund [ DMU 02/8 to M.G. and T.E., DID 02/35 to M.G., D.S. and G.M.].
Publisher Copyright:
© 2014 Elsevier Ltd.
PY - 2015/2
Y1 - 2015/2
N2 - 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.
AB - 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.
KW - Actin-related protein 4 (Arp4p)
KW - Chromatin
KW - Chromatin remodeling
KW - Hho1p
KW - higher-order chromatin structure
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U2 - 10.1016/j.biocel.2014.12.006
DO - 10.1016/j.biocel.2014.12.006
M3 - Article
C2 - 25542182
AN - SCOPUS:84920718646
VL - 59
SP - 182
EP - 192
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
SN - 1357-2725
ER -