| Structural highlights
Function
[RSC2_YEAST] Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in meiotic sporulation through regulating IME2 expression, and is also essential for 2-micron plasmid maintenance and for normal REP1 protein localization.[1] [2] [3] [4] [5] [6] [7] [8]
Publication Abstract from PubMed
Bromo-adjacent homology (BAH) domains are commonly found in chromatin-associated proteins and fall into two classes; Remodels the Structure of Chromatin (RSC)-like or Sir3-like. Although Sir3-like BAH domains bind nucleosomes, the binding partners of RSC-like BAH domains are currently unknown. The Rsc2 subunit of the RSC chromatin remodeling complex contains an RSC-like BAH domain and, like the Sir3-like BAH domains, we find Rsc2 BAH also interacts with nucleosomes. However, unlike Sir3-like BAH domains, we find that Rsc2 BAH can bind to recombinant purified H3 in vitro, suggesting that the mechanism of nucleosome binding is not conserved. To gain insight into the Rsc2 BAH domain, we determined its crystal structure at 2.4 A resolution. We find that it differs substantially from Sir3-like BAH domains and lacks the motifs in these domains known to be critical for making contacts with histones. We then go on to identify a novel motif in Rsc2 BAH that is critical for efficient H3 binding in vitro and show that mutation of this motif results in defective Rsc2 function in vivo. Moreover, we find this interaction is conserved across Rsc2-related proteins. These data uncover a binding target of the Rsc2 family of BAH domains and identify a novel motif that mediates this interaction.
The BAH domain of Rsc2 is a histone H3 binding domain.,Chambers AL, Pearl LH, Oliver AW, Downs JA Nucleic Acids Res. 2013 Jul 31. PMID:23907388[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wong MC, Scott-Drew SR, Hayes MJ, Howard PJ, Murray JA. RSC2, encoding a component of the RSC nucleosome remodeling complex, is essential for 2 microm plasmid maintenance in Saccharomyces cerevisiae. Mol Cell Biol. 2002 Jun;22(12):4218-29. PMID:12024034
- ↑ Cairns BR, Lorch Y, Li Y, Zhang M, Lacomis L, Erdjument-Bromage H, Tempst P, Du J, Laurent B, Kornberg RD. RSC, an essential, abundant chromatin-remodeling complex. Cell. 1996 Dec 27;87(7):1249-60. PMID:8980231
- ↑ Lorch Y, Zhang M, Kornberg RD. Histone octamer transfer by a chromatin-remodeling complex. Cell. 1999 Feb 5;96(3):389-92. PMID:10025404
- ↑ Moreira JM, Holmberg S. Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC. EMBO J. 1999 May 17;18(10):2836-44. PMID:10329629 doi:10.1093/emboj/18.10.2836
- ↑ Yukawa M, Koyama H, Miyahara K, Tsuchiya E. Functional differences between RSC1 and RSC2, components of a for growth essential chromatin-remodeling complex of Saccharomyces cerevisiae, during the sporulation process. FEMS Yeast Res. 2002 May;2(2):87-91. PMID:12702296
- ↑ Saha A, Wittmeyer J, Cairns BR. Chromatin remodeling by RSC involves ATP-dependent DNA translocation. Genes Dev. 2002 Aug 15;16(16):2120-34. PMID:12183366 doi:10.1101/gad.995002
- ↑ Chai B, Hsu JM, Du J, Laurent BC. Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway. Genetics. 2002 Jun;161(2):575-84. PMID:12072455
- ↑ Hsu JM, Huang J, Meluh PB, Laurent BC. The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation. Mol Cell Biol. 2003 May;23(9):3202-15. PMID:12697820
- ↑ Chambers AL, Pearl LH, Oliver AW, Downs JA. The BAH domain of Rsc2 is a histone H3 binding domain. Nucleic Acids Res. 2013 Jul 31. PMID:23907388 doi:10.1093/nar/gkt662
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