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. 2021 Mar;31(3):426–435. doi: 10.1101/gr.266510.120

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© 2021 Frenkel et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see https://genome.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — Rtt109 acts via H3 N-terminal acetylation to reduce fork velocity. (A) Genetic interaction between histone N-terminal acetylation and Rtt109 or SAGA/SLIK complexes. Relative replicon length change (log₂) after an N-terminal substitution (4KQ, open circle; 4KA, closed circle) in wt (gray), RTT109-deleted (blue), or SAGA-HAT-core subunit-deleted (pink) cells is plotted against their replicon length (x-axis in log scale). (B) Genetic interactions between RTT109 and histone acetylation during DNA replication. For each lysine H3 N-terminal and K56 substitution (naming as in Figs. 3A, 4A), and their combinations, the relative replicon length (log₂) after RTT109 deletion is plotted against its replicon length without RTT109 deletion. Gray indicates wt; red, H3K56 substitutions; green, N-terminal substitutions; purple, combined H3K56 and N-terminal substitutions; x-axis in log scale. (C) Synergistic effect of H3K56 and H3 N-terminal substitutions on DNA replication dynamics. The replicon lengths of mutants with combinations of H3K56 (columns) and H3 N-terminal 4K (rows) substitutions are shown. Colored squares indicate the replicon length after combining N-terminal mutation; gray squares indicate missing data for 4KR + K56A. (D) A working model: Histone H3 N-terminal acetylation by Rtt109 promotes nucleosome deposition in front of the fork and thus slows DNA replication.