Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis

J. Recht; T. Tsubota; J. C. Tanny; R. L. Diaz; J. M. Berger; X. Zhang; B. A. Garcia; J. Shabanowitz; A. L. Burlingame; D. F. Hunt; P. D. Kaufman; C. D. Allis

doi:10.1073/pnas.0601676103

Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis

J. Recht, T. Tsubota, J. C. Tanny, R. L. Diaz, J. M. Berger, X. Zhang, B. A. Garcia, J. Shabanowitz, A. L. Burlingame, D. F. Hunt, P. D. Kaufman, C. D. Allis

Research output: Contribution to journal › Article › peer-review

199 Scopus citations

Abstract

Histone acetylation affects many nuclear processes including transcription, chromatin assembly, and DNA damage repair. Acetylation of histone H3 lysine 56 (H3 K56ac) in budding yeast occurs during mitotic 5 phase and persists during DNA damage repair. Here, we show that H3 K56ac is also present during premeiotic S phase and is conserved in fission yeast. Furthermore, the H3 K56ac modification is not observed in the absence of the histone chaperone Asf1. asf1Δ and H3 K56R mutants exhibit similar sensitivity to DNA damaging agents. Mutational analysis of Asf1 demonstrates that DNA damage sensitivity correlates with (i) decreased levels of H3 K56ac and (ii) a region implicated in histone binding. In contrast, multiple asf1 mutants that are resistant to DNA damage display WT levels of K56ac. These data suggest that maintenance of H3 K56 acetylation is a primary contribution of Asf1 to genome stability in yeast.

Original language	English (US)
Pages (from-to)	6988-6993
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	103
Issue number	18
DOIs	https://doi.org/10.1073/pnas.0601676103
State	Published - May 2 2006
Externally published	Yes

Keywords

Chromatin assembly
DNA damage
H3 K56ac

ASJC Scopus subject areas

General

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10.1073/pnas.0601676103

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Recht, J., Tsubota, T., Tanny, J. C., Diaz, R. L., Berger, J. M., Zhang, X., Garcia, B. A., Shabanowitz, J., Burlingame, A. L., Hunt, D. F., Kaufman, P. D., & Allis, C. D. (2006). Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis. Proceedings of the National Academy of Sciences of the United States of America, 103(18), 6988-6993. https://doi.org/10.1073/pnas.0601676103

Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis. / Recht, J.; Tsubota, T.; Tanny, J. C. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 18, 02.05.2006, p. 6988-6993.

Research output: Contribution to journal › Article › peer-review

Recht, J, Tsubota, T, Tanny, JC, Diaz, RL, Berger, JM, Zhang, X, Garcia, BA, Shabanowitz, J, Burlingame, AL, Hunt, DF, Kaufman, PD & Allis, CD 2006, 'Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis', Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 18, pp. 6988-6993. https://doi.org/10.1073/pnas.0601676103

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abstract = "Histone acetylation affects many nuclear processes including transcription, chromatin assembly, and DNA damage repair. Acetylation of histone H3 lysine 56 (H3 K56ac) in budding yeast occurs during mitotic 5 phase and persists during DNA damage repair. Here, we show that H3 K56ac is also present during premeiotic S phase and is conserved in fission yeast. Furthermore, the H3 K56ac modification is not observed in the absence of the histone chaperone Asf1. asf1Δ and H3 K56R mutants exhibit similar sensitivity to DNA damaging agents. Mutational analysis of Asf1 demonstrates that DNA damage sensitivity correlates with (i) decreased levels of H3 K56ac and (ii) a region implicated in histone binding. In contrast, multiple asf1 mutants that are resistant to DNA damage display WT levels of K56ac. These data suggest that maintenance of H3 K56 acetylation is a primary contribution of Asf1 to genome stability in yeast.",

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AB - Histone acetylation affects many nuclear processes including transcription, chromatin assembly, and DNA damage repair. Acetylation of histone H3 lysine 56 (H3 K56ac) in budding yeast occurs during mitotic 5 phase and persists during DNA damage repair. Here, we show that H3 K56ac is also present during premeiotic S phase and is conserved in fission yeast. Furthermore, the H3 K56ac modification is not observed in the absence of the histone chaperone Asf1. asf1Δ and H3 K56R mutants exhibit similar sensitivity to DNA damaging agents. Mutational analysis of Asf1 demonstrates that DNA damage sensitivity correlates with (i) decreased levels of H3 K56ac and (ii) a region implicated in histone binding. In contrast, multiple asf1 mutants that are resistant to DNA damage display WT levels of K56ac. These data suggest that maintenance of H3 K56 acetylation is a primary contribution of Asf1 to genome stability in yeast.

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Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitois and meiosis

Abstract

Keywords

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