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Rtt109 slows replication speed by histone N-terminal acetylation
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| Zeitschriftentitel: | Genome Research |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Genome Research, 31, 2021, 3, S. 426-435 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama |
|---|---|
| author |
Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama |
| spellingShingle |
Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama Genome Research Rtt109 slows replication speed by histone N-terminal acetylation Genetics (clinical) Genetics |
| author_sort |
frenkel, nelly |
| spelling |
Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama 1088-9051 1549-5469 Cold Spring Harbor Laboratory Genetics (clinical) Genetics http://dx.doi.org/10.1101/gr.266510.120 <jats:p>The wrapping of DNA around histone octamers challenges processes that use DNA as their template. In vitro, DNA replication through chromatin depends on histone modifiers, raising the possibility that cells modify histones to optimize fork progression. Rtt109 is an acetyl transferase that acetylates histone H3 before its DNA incorporation on the K56 and N-terminal residues. We previously reported that, in budding yeast, a wave of histone H3 K9 acetylation progresses ∼3–5 kb ahead of the replication fork. Whether this wave contributes to replication dynamics remained unknown. Here, we show that the replication fork velocity increases following deletion of<jats:italic>RTT109</jats:italic>, the gene encoding the enzyme required for the prereplication H3 acetylation wave. By using histone H3 mutants, we find that Rtt109-dependent N-terminal acetylation regulates fork velocity, whereas K56 acetylation contributes to replication dynamics only when N-terminal acetylation is compromised. We propose that acetylation of newly synthesized histones slows replication by promoting replacement of nucleosomes evicted by the incoming fork, thereby protecting genome integrity.</jats:p> Rtt109 slows replication speed by histone N-terminal acetylation Genome Research |
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Cold Spring Harbor Laboratory, 2021 |
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| title |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_unstemmed |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_full |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_fullStr |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_full_unstemmed |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_short |
Rtt109 slows replication speed by histone N-terminal acetylation |
| title_sort |
rtt109 slows replication speed by histone n-terminal acetylation |
| topic |
Genetics (clinical) Genetics |
| url |
http://dx.doi.org/10.1101/gr.266510.120 |
| publishDate |
2021 |
| physical |
426-435 |
| description |
<jats:p>The wrapping of DNA around histone octamers challenges processes that use DNA as their template. In vitro, DNA replication through chromatin depends on histone modifiers, raising the possibility that cells modify histones to optimize fork progression. Rtt109 is an acetyl transferase that acetylates histone H3 before its DNA incorporation on the K56 and N-terminal residues. We previously reported that, in budding yeast, a wave of histone H3 K9 acetylation progresses ∼3–5 kb ahead of the replication fork. Whether this wave contributes to replication dynamics remained unknown. Here, we show that the replication fork velocity increases following deletion of<jats:italic>RTT109</jats:italic>, the gene encoding the enzyme required for the prereplication H3 acetylation wave. By using histone H3 mutants, we find that Rtt109-dependent N-terminal acetylation regulates fork velocity, whereas K56 acetylation contributes to replication dynamics only when N-terminal acetylation is compromised. We propose that acetylation of newly synthesized histones slows replication by promoting replacement of nucleosomes evicted by the incoming fork, thereby protecting genome integrity.</jats:p> |
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| author | Frenkel, Nelly, Jonas, Felix, Carmi, Miri, Yaakov, Gilad, Barkai, Naama |
| author_facet | Frenkel, Nelly, Jonas, Felix, Carmi, Miri, Yaakov, Gilad, Barkai, Naama, Frenkel, Nelly, Jonas, Felix, Carmi, Miri, Yaakov, Gilad, Barkai, Naama |
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| description | <jats:p>The wrapping of DNA around histone octamers challenges processes that use DNA as their template. In vitro, DNA replication through chromatin depends on histone modifiers, raising the possibility that cells modify histones to optimize fork progression. Rtt109 is an acetyl transferase that acetylates histone H3 before its DNA incorporation on the K56 and N-terminal residues. We previously reported that, in budding yeast, a wave of histone H3 K9 acetylation progresses ∼3–5 kb ahead of the replication fork. Whether this wave contributes to replication dynamics remained unknown. Here, we show that the replication fork velocity increases following deletion of<jats:italic>RTT109</jats:italic>, the gene encoding the enzyme required for the prereplication H3 acetylation wave. By using histone H3 mutants, we find that Rtt109-dependent N-terminal acetylation regulates fork velocity, whereas K56 acetylation contributes to replication dynamics only when N-terminal acetylation is compromised. We propose that acetylation of newly synthesized histones slows replication by promoting replacement of nucleosomes evicted by the incoming fork, thereby protecting genome integrity.</jats:p> |
| doi_str_mv | 10.1101/gr.266510.120 |
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| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105 |
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| spelling | Frenkel, Nelly Jonas, Felix Carmi, Miri Yaakov, Gilad Barkai, Naama 1088-9051 1549-5469 Cold Spring Harbor Laboratory Genetics (clinical) Genetics http://dx.doi.org/10.1101/gr.266510.120 <jats:p>The wrapping of DNA around histone octamers challenges processes that use DNA as their template. In vitro, DNA replication through chromatin depends on histone modifiers, raising the possibility that cells modify histones to optimize fork progression. Rtt109 is an acetyl transferase that acetylates histone H3 before its DNA incorporation on the K56 and N-terminal residues. We previously reported that, in budding yeast, a wave of histone H3 K9 acetylation progresses ∼3–5 kb ahead of the replication fork. Whether this wave contributes to replication dynamics remained unknown. Here, we show that the replication fork velocity increases following deletion of<jats:italic>RTT109</jats:italic>, the gene encoding the enzyme required for the prereplication H3 acetylation wave. By using histone H3 mutants, we find that Rtt109-dependent N-terminal acetylation regulates fork velocity, whereas K56 acetylation contributes to replication dynamics only when N-terminal acetylation is compromised. We propose that acetylation of newly synthesized histones slows replication by promoting replacement of nucleosomes evicted by the incoming fork, thereby protecting genome integrity.</jats:p> Rtt109 slows replication speed by histone N-terminal acetylation Genome Research |
| spellingShingle | Frenkel, Nelly, Jonas, Felix, Carmi, Miri, Yaakov, Gilad, Barkai, Naama, Genome Research, Rtt109 slows replication speed by histone N-terminal acetylation, Genetics (clinical), Genetics |
| title | Rtt109 slows replication speed by histone N-terminal acetylation |
| title_full | Rtt109 slows replication speed by histone N-terminal acetylation |
| title_fullStr | Rtt109 slows replication speed by histone N-terminal acetylation |
| title_full_unstemmed | Rtt109 slows replication speed by histone N-terminal acetylation |
| title_short | Rtt109 slows replication speed by histone N-terminal acetylation |
| title_sort | rtt109 slows replication speed by histone n-terminal acetylation |
| title_unstemmed | Rtt109 slows replication speed by histone N-terminal acetylation |
| topic | Genetics (clinical), Genetics |
| url | http://dx.doi.org/10.1101/gr.266510.120 |