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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Luger, Karolin Hepler, Maggie R. D. Hieb, Aaron R. Clark, Nicholas J. Yao, Tingting Muthurajan, Uma M. Kramer, Michael |
| Description | Author Affiliation: Muthurajan UM ( Department of Biochemistry and Molecular Biology, and.); Hepler MR ( Department of Biochemistry and Molecular Biology, and.); Hieb AR ( Department of Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO 80523-1870.); Clark NJ ( Department of Biochemistry and Molecular Biology, and.); Kramer M ( Department of Biochemistry and Molecular Biology, and.); Yao T ( Department of Biochemistry and Molecular Biology, and.); Luger K ( Department of Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, Colorado State University, Fort Collins, CO 80523-1870 kluger@lamar.colostate.edu.); |
| Abstract | Poly [ADP-ribose] polymerase 1 (PARP-1) is a highly abundant chromatin-associated enzyme. It catalyzes the NAD(+)-dependent polymerization of long chains of poly-ADP ribose (PAR) onto itself in response to DNA damage and other cues. More recently, the enzymatic activity of PARP-1 has also been implicated in the regulation of gene expression. The molecular basis for the functional switch from chromatin architectural protein to transcription factor and DNA damage responder, triggered by PARP-1 automodification, is unknown. Here, we show that unmodified PARP-1 engages in at least two high-affinity binding modes with chromatin, one of which does not involve free DNA ends, consistent with its role as a chromatin architectural protein. Automodification reduces PARP-1 affinity for intact chromatin but not for nucleosomes with exposed DNA ends. Automodified (AM) PARP-1 has the ability to sequester histones (both in vitro and in cells) and to assemble nucleosomes efficiently in vitro. This unanticipated nucleosome assembly activity of AM-PARP-1, coupled with the fast turnover of the modification, suggests a model in which DNA damage or transcription events trigger transient histone chaperone activity. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 35 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Chromatin Metabolism Histone Chaperones Poly(ADP-ribose) Polymerases Chemistry DNA Damage Physiology DNA Repair Fluorescence Resonance Energy Transfer Nucleosomes Genetics Protein Binding Protein Processing, Post-Translational Transcription, Genetic Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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