Structure and dynamic properties of nucleosome core particles.
It is now widely recognized that the packaging of genomic DNA, together with core histones, linker histones, and other functional proteins into chromatin profoundly influences nuclear processes such as transcription, replication, DNA repair, and recombination. Whereas earlier structural studies portrayed nucleosomes (the basic repeating unit of chromatin) as monolithic and static macromolecular assemblies, we now know that they are highly dynamic and capable of extensive crosstalk with the cellular machinery. Histone variants have evolved to locally alter chromatin structure, whereas histone chaperones and other cellular factors promote histone exchange and chromatin fluidity. Both of these phenomena likely facilitate interconversion between different chromatin states that show varying degrees of transcriptional activity.
Chakravarthy
Srinivas
S
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Park
Young-Jun
YJ
Chodaparambil
Jayanth
J
Edayathumangalam
Rajeswari S
RS
Luger
Karolin
K
D000818:Animals; D003461:Crystallography; D004247:DNA / Q000737:chemistry; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D018832:Molecular Chaperones / Q000502:physiology*; D015394:Molecular Structure; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism*
D006657:Histones; D018832:Molecular Chaperones; D009707:Nucleosomes; D004247:DNA