In this section
@article{Jalal:2024:10.1016/j.molcel.2024.08.015,
author = {Jalal, ASB and Girvan, P and Chua, EYD and Liu, L and Wang, S and McCormack, EA and Skehan, MT and Knight, CL and Rueda, DS and Wigley, DB},
doi = {10.1016/j.molcel.2024.08.015},
journal = {Molecular Cell},
pages = {3871--3884.e9},
title = {Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex},
url = {http://dx.doi.org/10.1016/j.molcel.2024.08.015},
volume = {84},
year = {2024}
}
TY - JOUR
AB - The yeast SWR1 complex catalyzes the exchange of histone H2A/H2B dimers in nucleosomes with Htz1/H2B dimers. We use cryoelectron microscopy to determine the structure of an enzyme-bound hexasome intermediate in the reaction pathway of histone exchange, in which an H2A/H2B dimer has been extracted from a nucleosome prior to the insertion of a dimer comprising Htz1/H2B. The structure reveals a key role for the Swc5 subunit in stabilizing the unwrapping of DNA from the histone core of the hexasome. By engineering a crosslink between an Htz1/H2B dimer and its chaperone protein Chz1, we show that this blocks histone exchange by SWR1 but allows the incoming chaperone-dimer complex to insert into the hexasome. We use this reagent to trap an SWR1/hexasome complex with an incoming Htz1/H2B dimer that shows how the reaction progresses to the next step. Taken together the structures reveal insights into the mechanism of histone exchange by SWR1 complex.
AU - Jalal,ASB
AU - Girvan,P
AU - Chua,EYD
AU - Liu,L
AU - Wang,S
AU - McCormack,EA
AU - Skehan,MT
AU - Knight,CL
AU - Rueda,DS
AU - Wigley,DB
DO - 10.1016/j.molcel.2024.08.015
EP - 3884
PY - 2024///
SN - 1097-2765
SP - 3871
TI - Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex
T2 - Molecular Cell
UR - http://dx.doi.org/10.1016/j.molcel.2024.08.015
VL - 84
ER -