The nucleosome repeating unit of chromatin is the target of chromatin enzymes and factors that regulate gene activity in a eukaryotic cell. How the nucleosome is recognized by chromatin enzymes and factors is poorly understood, even though such interaction is fundamental to gene regulation and chromatin biology. My laboratory recently determined the structural basis for how the RCC1 (regulator of chromosome condensation 1) chromatin factor binds to the nucleosome, including the first atomic crystal structure of a chromatin protein complexed with the nucleosome core particle. I describe here how we developed and investigated structural models for RCC1 binding to the nucleosome using biochemical methods and how we crystallized the 300 kDa complex of RCC1 with the nucleosome core particle. This article highlights the contributions made by key laboratory members and explains our thinking and rationale during the discovery process.
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April 2012
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Conference Article|
March 21 2012
Deciphering how the chromatin factor RCC1 recognizes the nucleosome: the importance of individuals in the scientific discovery process
Song Tan
Song Tan
1
1Center for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, Pennsylvania State University, University Park, PA 16802-1014, U.S.A.
1emailsxt30@psu.edu
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Publisher: Portland Press Ltd
Received:
September 06 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem Soc Trans (2012) 40 (2): 351–356.
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Received:
September 06 2011
Citation
Song Tan; Deciphering how the chromatin factor RCC1 recognizes the nucleosome: the importance of individuals in the scientific discovery process. Biochem Soc Trans 1 April 2012; 40 (2): 351–356. doi: https://doi.org/10.1042/BST20110734
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