Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

TY - JOUR

T1 - Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

AU - Zhang, Wei

AU - Yyl, Marek

AU - Ward, Richard

AU - Sobott, Frank

AU - Maman, Joseph

AU - Murthy, Andal

AU - Watson, Aleksandra

AU - Fedorov, Oleg

AU - Bowman, Andrew

AU - Owen-Hughes, Tom

AU - El Mkami, Hassane

AU - Murzina, Natalia

AU - Norman, David G

AU - Laue, Ernest

PY - 2013/1

Y1 - 2013/1

N2 - The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.

AB - The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.

KW - RbAp48

KW - ASF1

KW - EPR spectroscopy

KW - HISTONE CHAPERONE

UR - https://www.scopus.com/pages/publications/84872031844

U2 - 10.1038/nsmb.2446

DO - 10.1038/nsmb.2446

M3 - Article

C2 - 23178455

AN - SCOPUS:84872031844

SN - 1545-9993

VL - 20

SP - 29

EP - 35

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 1

ER -