@article{Willhoft:2016:nar/gkw509,
author = {Willhoft, O and Bythell-Douglas, R and Mccormack, EA and Wigley, DB},
doi = {nar/gkw509},
journal = {Nucleic Acids Research},
pages = {8179--8188},
title = {Synergy and antagonism in regulation of recombinant human INO80 chromatin remodeling complex},
url = {http://dx.doi.org/10.1093/nar/gkw509},
volume = {44},
year = {2016}
}

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TY  - JOUR
AB  - We have purified a minimal core human Ino80 complex from recombinant protein expressedin insect cells. The complex comprises one subunit each of an N-terminally truncated Ino80,actin, Arp4, Arp5, Arp8, Ies2 and Ies6, together with a single heterohexamer of the Tip49aand Tip49b proteins. This core complex has nucleosome sliding activity that is similar to thatof endogenous human and yeast Ino80 complexes and is also inhibited by inositolhexaphosphate (IP6). We show that IP6 is a non-competitive inhibitor that acts by blockingthe stimulatory effect of nucleosomes on the ATPase activity. The IP6 binding site is locatedwithin the C-terminal region of the Ino80 subunit. We have also prepared complexes lackingcombinations of Ies2 and Arp5/Ies6 subunits that reveal regulation imposed by each of themindividually and synergistically that couples ATP hydrolysis to nucleosome sliding. Thiscoupling between Ies2 and Arp5/Ies6 can be overcome in a bypass mutation of the Arp5subunit that is active in the absence of Ies2. These studies reveal several underlyingmechanisms for regulation of ATPase activity involving a complex interplay between theseprotein subunits and IP6 that in turn controls nucleosome sliding.
AU  - Willhoft,O
AU  - Bythell-Douglas,R
AU  - Mccormack,EA
AU  - Wigley,DB
DO  - nar/gkw509
EP  - 8188
PY  - 2016///
SN  - 1362-4962
SP  - 8179
TI  - Synergy and antagonism in regulation of recombinant human INO80 chromatin remodeling complex
T2  - Nucleic Acids Research
UR  - http://dx.doi.org/10.1093/nar/gkw509
UR  - https://academic.oup.com/nar/article/44/17/8179/2468024
UR  - http://hdl.handle.net/10044/1/33251
VL  - 44
ER  - 

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