The ISWI class of proteins consists of a family of chromatin remodeling ATPases that is ubiquitous in eukaryotes and predominantly functions to slide nucleosomes laterally. The yeast Saccharomyces cerevisiae Isw1 partners with several non-essential alternative subunits — Ioc2, Ioc3, or Ioc4 — to form two distinct complexes Isw1a and Isw1b. Besides its ATPase domain, Isw1 presents a C-terminal region formed by HAND, SANT, and SLIDE domains responsible for interaction with the Ioc proteins and optimal association of Isw1 to chromatin. Despite diverse studies on the functions of the Isw1-containing complexes, molecular evidence for a regulation of this chromatin remodeling ATPase is still elusive. Results presented here indicate that Isw1 is not only ubiquitylated but also strongly SUMOylated on multiple lysine residues by the redundant Siz1/Siz2 SUMO E3 ligases. However, Isw1 is a poor substrate of the Ulp1 and Ulp2 SUMO proteases, thus resulting in a high level of modification. Extensive site-directed mutagenesis allowed us to identify the major SUMOylation sites and develop a SUMO-defective mutant of Isw1. Using this molecular tool, we show that SUMOylation of Isw1 specifically facilitates and/or stabilizes its interaction with its cofactor Ioc3 and consequently the efficient recruitment of the Isw1–Ioc3 complex onto chromatin. Together these data reveal a new regulatory mechanism for this fascinating remodeling factor.
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October 2017
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Nuclear localization of aryl hydrocarbon receptor (AhR) in HepG2 cells treated with Carbidopa. The green fluorescence signal for AhR is overlayed with the blue fluorescence (DAPI) signal for the nucleus, showing complete translocation of AhR from cytoplasm into nucleus. In this issue of the Biochemical Journal, Ogura et al, report on the potential role of Carbidopa in cancer therapy (pages 3391–3402).
Research Article|
October 05 2017
The chromatin remodeling Isw1a complex is regulated by SUMOylation
Qingtang Shen;
Qingtang Shen
1University Paris Diderot, Sorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Hôpital St. Louis, 1 Avenue Claude Vellefaux, 75475 Paris Cedex 10, France
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Nissrine Beyrouthy;
Nissrine Beyrouthy
1University Paris Diderot, Sorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Hôpital St. Louis, 1 Avenue Claude Vellefaux, 75475 Paris Cedex 10, France
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Laura Matabishi-Bibi;
Laura Matabishi-Bibi
1University Paris Diderot, Sorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Hôpital St. Louis, 1 Avenue Claude Vellefaux, 75475 Paris Cedex 10, France
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Catherine Dargemont
1University Paris Diderot, Sorbonne Paris Cité, INSERM UMR944, CNRS UMR7212, Hôpital St. Louis, 1 Avenue Claude Vellefaux, 75475 Paris Cedex 10, France
Correspondence: Catherine Dargemont (catherine.dargemont@inserm.fr)
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Publisher: Portland Press Ltd
Received:
March 03 2017
Revision Received:
August 29 2017
Accepted:
September 08 2017
Accepted Manuscript online:
September 12 2017
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem J (2017) 474 (20): 3455–3469.
Article history
Received:
March 03 2017
Revision Received:
August 29 2017
Accepted:
September 08 2017
Accepted Manuscript online:
September 12 2017
Citation
Qingtang Shen, Nissrine Beyrouthy, Laura Matabishi-Bibi, Catherine Dargemont; The chromatin remodeling Isw1a complex is regulated by SUMOylation. Biochem J 15 October 2017; 474 (20): 3455–3469. doi: https://doi.org/10.1042/BCJ20170172
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