OpinionThe linker-protein network: control of nucleosomal DNA accessibility
Review articleOpen access
2008/06/01 Full-length article DOI: 10.1016/j.tibs.2008.04.001
Journal: Trends in Biochemical Sciences
Numerous studies have recently addressed the accessibility of nucleosomal DNA to protein factors. Two popular concepts – the histone code and chromatin remodeling – consider the nucleosome as a passive entity that ‘waits’ to be marked by histone modifications and is ‘mobilized’ by ATP-dependent remodelers. Here, we propose a holistic view of the nucleosome as an active, dynamic entity, the accessibility of which is controlled by binding of different linker proteins to the DNA entry/exit site. The linker proteins might directly compete for this binding site; alternatively, protein chaperones and/or chromatin remodelers might exchange one linker protein for another. Finally, according to our proposed model, the exchange factors are themselves controlled by post-translational modifications or binding of protein partners, to respond to the ever-changing intra- and extra-cellular environment.
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