The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation

TY - JOUR

T1 - The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation

A1 - Bowman,A.

A1 - Ward,Richard

A1 - Wiechens,Nicola

A1 - Singh,Vijender

A1 - El-Mkami,Hassane

A1 - Norman,David George

A1 - Owen-Hughes,Tom

AU - Bowman,A.

AU - Ward,Richard

AU - Wiechens,Nicola

AU - Singh,Vijender

AU - El-Mkami,Hassane

AU - Norman,David George

AU - Owen-Hughes,Tom

PY - 2011/2/18

Y1 - 2011/2/18

N2 - <p>Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.</p>

AB - <p>Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.</p>

KW - NUCLEOSOME ASSEMBLY PROTEIN-1

KW - DNA-REPLICATION

KW - ACETYLTRANSFERASE RTT109

KW - CRYSTAL-STRUCTURE

KW - STRUCTURAL BASIS

KW - COMPLEXES

KW - CORE

KW - CHROMATIN

KW - ACETYLATION

KW - ASF1

UR - http://ukpmc.ac.uk/articles/PMC3093613

U2 - 10.1016/j.molcel.2011.01.025

DO - 10.1016/j.molcel.2011.01.025

M1 - Article

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

VL - 41

SP - 398

EP - 408

ER -