Replication stress interferes with histone recycling and predeposition marking of new histones
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Replication stress interferes with histone recycling and predeposition marking of new histones. / Jasencakova, Zuzana; Scharf, Annette N D; Ask, Katrine; Corpet, Armelle; Imhof, Axel; Almouzni, Geneviève; Groth, Anja.
In: Molecular Cell, Vol. 37, No. 5, 12.03.2010, p. 736-43.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Replication stress interferes with histone recycling and predeposition marking of new histones
AU - Jasencakova, Zuzana
AU - Scharf, Annette N D
AU - Ask, Katrine
AU - Corpet, Armelle
AU - Imhof, Axel
AU - Almouzni, Geneviève
AU - Groth, Anja
N1 - Paper id:: 10.1016/j.molcel.2010.01.033
PY - 2010/3/12
Y1 - 2010/3/12
N2 - To restore chromatin on new DNA during replication, recycling of histones evicted ahead of the fork is combined with new histone deposition. The Asf1 histone chaperone, which buffers excess histones under stress, is a key player in this process. Yet how histones handled by human Asf1 are modified remains unclear. Here we identify marks on histones H3-H4 bound to Asf1 and changes induced upon replication stress. In S phase, distinct cytosolic and nuclear Asf1b complexes show ubiquitous H4K5K12diAc and heterogeneous H3 marks, including K9me1, K14ac, K18ac, and K56ac. Upon acute replication arrest, the predeposition mark H3K9me1 and modifications typical of chromatin accumulate in Asf1 complexes. In parallel, ssDNA is generated at replication sites, consistent with evicted histones being trapped with Asf1. During recovery, histones stored with Asf1 are rapidly used as replication resumes. This shows that replication stress interferes with predeposition marking and histone recycling with potential impact on epigenetic stability.
AB - To restore chromatin on new DNA during replication, recycling of histones evicted ahead of the fork is combined with new histone deposition. The Asf1 histone chaperone, which buffers excess histones under stress, is a key player in this process. Yet how histones handled by human Asf1 are modified remains unclear. Here we identify marks on histones H3-H4 bound to Asf1 and changes induced upon replication stress. In S phase, distinct cytosolic and nuclear Asf1b complexes show ubiquitous H4K5K12diAc and heterogeneous H3 marks, including K9me1, K14ac, K18ac, and K56ac. Upon acute replication arrest, the predeposition mark H3K9me1 and modifications typical of chromatin accumulate in Asf1 complexes. In parallel, ssDNA is generated at replication sites, consistent with evicted histones being trapped with Asf1. During recovery, histones stored with Asf1 are rapidly used as replication resumes. This shows that replication stress interferes with predeposition marking and histone recycling with potential impact on epigenetic stability.
KW - Acetylation
KW - Blotting, Western
KW - Cell Cycle Proteins
KW - Cell Nucleus
KW - Chromatin Assembly and Disassembly
KW - Cytosol
KW - DNA Replication
KW - DNA, Single-Stranded
KW - Hela Cells
KW - Histones
KW - Humans
KW - Methylation
KW - Nuclear Proteins
KW - Nucleosomes
KW - Protein Binding
KW - Protein Processing, Post-Translational
KW - S Phase
KW - Stress, Physiological
KW - Tandem Mass Spectrometry
KW - Time Factors
KW - Transfection
U2 - 10.1016/j.molcel.2010.01.033
DO - 10.1016/j.molcel.2010.01.033
M3 - Journal article
C2 - 20227376
VL - 37
SP - 736
EP - 743
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 5
ER -
ID: 21235048