Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

Aaron J. Gottschalk; Gyula Timinszky; Stephanie E. Kong; Jingji Jin; Yong Cai; Selene K. Swanson; Michael P. Washburn; Laurence Florens; Andreas G. Ladurner; Joan W. Conaway; Ronald C. Conaway

doi:10.1073/pnas.0906920106

Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

Aaron J. Gottschalk, Gyula Timinszky, Stephanie E. Kong, Jingji Jin, Yong Cai, Selene K. Swanson, Michael P. Washburn, Laurence Florens, Andreas G. Ladurner, Joan W. Conaway, Ronald C. Conaway

Research output: Contribution to journal › Article › peer-review

299 Scopus citations

Abstract

Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl) ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.

Original language	English (US)
Pages (from-to)	13770-13774
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	106
Issue number	33
DOIs	https://doi.org/10.1073/pnas.0906920106
State	Published - Aug 18 2009
Externally published	Yes

Keywords

Alc1
Chromatin remodeling enzyme
Macrodomain
Poly-(ADP-ribose) polymerase
Snf2-like ATPase

ASJC Scopus subject areas

General

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10.1073/pnas.0906920106

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Gottschalk, A. J., Timinszky, G., Kong, S. E., Jin, J., Cai, Y., Swanson, S. K., Washburn, M. P., Florens, L., Ladurner, A. G., Conaway, J. W., & Conaway, R. C. (2009). Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler. Proceedings of the National Academy of Sciences of the United States of America, 106(33), 13770-13774. https://doi.org/10.1073/pnas.0906920106

Gottschalk, AJ, Timinszky, G, Kong, SE, Jin, J, Cai, Y, Swanson, SK, Washburn, MP, Florens, L, Ladurner, AG, Conaway, JW & Conaway, RC 2009, 'Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler', Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 33, pp. 13770-13774. https://doi.org/10.1073/pnas.0906920106

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abstract = "Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl) ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.",

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AU - Cai, Yong

AU - Swanson, Selene K.

AU - Washburn, Michael P.

AU - Florens, Laurence

AU - Ladurner, Andreas G.

AU - Conaway, Joan W.

AU - Conaway, Ronald C.

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N2 - Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl) ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.

AB - Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl) ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.

KW - Alc1

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KW - Macrodomain

KW - Poly-(ADP-ribose) polymerase

KW - Snf2-like ATPase

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Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

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