Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication

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Standard

Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication. / Kamalyukova, Ilnaz M; Young, Clifford; Strømme, Caroline B; Menard, Patrice; Jasencakova, Zusana; Mejlvang, Jakob; Ask, Katrine; Ploug, Michael; Nielsen, Michael L; Jensen, Ole N; Groth, Anja.

In: Nature Communications, Vol. 5, 2014, p. 3394.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kamalyukova, IM, Young, C, Strømme, CB, Menard, P, Jasencakova, Z, Mejlvang, J, Ask, K, Ploug, M, Nielsen, ML, Jensen, ON & Groth, A 2014, 'Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication', Nature Communications, vol. 5, pp. 3394. https://doi.org/10.1038/ncomms4394

APA

Kamalyukova, I. M., Young, C., Strømme, C. B., Menard, P., Jasencakova, Z., Mejlvang, J., Ask, K., Ploug, M., Nielsen, M. L., Jensen, O. N., & Groth, A. (2014). Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication. Nature Communications, 5, 3394. https://doi.org/10.1038/ncomms4394

Vancouver

Kamalyukova IM, Young C, Strømme CB, Menard P, Jasencakova Z, Mejlvang J et al. Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication. Nature Communications. 2014;5:3394. https://doi.org/10.1038/ncomms4394

Author

Kamalyukova, Ilnaz M ; Young, Clifford ; Strømme, Caroline B ; Menard, Patrice ; Jasencakova, Zusana ; Mejlvang, Jakob ; Ask, Katrine ; Ploug, Michael ; Nielsen, Michael L ; Jensen, Ole N ; Groth, Anja. / Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication. In: Nature Communications. 2014 ; Vol. 5. pp. 3394.

Bibtex

@article{a6b295d488d14a0280c8261251c4594d,
title = "Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication",
abstract = "During DNA replication, nucleosomes are rapidly assembled on newly synthesized DNA to restore chromatin organization. Asf1, a key histone H3-H4 chaperone required for this process, is phosphorylated by Tousled-like kinases (TLKs). Here, we identify TLK phosphorylation sites by mass spectrometry and dissect how phosphorylation has an impact on human Asf1 function. The divergent C-terminal tail of Asf1a is phosphorylated at several sites, and this is required for timely progression through S phase. Consistent with this, biochemical analysis of wild-type and phospho-mimetic Asf1a shows that phosphorylation enhances binding to histones and the downstream chaperones CAF-1 and HIRA. Moreover, we find that TLK phosphorylation of Asf1a is induced in cells experiencing deficiency of new histones and that TLK interaction with Asf1a involves its histone-binding pocket. We thus propose that TLK signalling promotes histone supply in S phase by targeting histone-free Asf1 and stimulating its ability to shuttle histones to sites of chromatin assembly.",
author = "Kamalyukova, {Ilnaz M} and Clifford Young and Str{\o}mme, {Caroline B} and Patrice Menard and Zusana Jasencakova and Jakob Mejlvang and Katrine Ask and Michael Ploug and Nielsen, {Michael L} and Jensen, {Ole N} and Anja Groth",
year = "2014",
doi = "10.1038/ncomms4394",
language = "English",
volume = "5",
pages = "3394",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication

AU - Kamalyukova, Ilnaz M

AU - Young, Clifford

AU - Strømme, Caroline B

AU - Menard, Patrice

AU - Jasencakova, Zusana

AU - Mejlvang, Jakob

AU - Ask, Katrine

AU - Ploug, Michael

AU - Nielsen, Michael L

AU - Jensen, Ole N

AU - Groth, Anja

PY - 2014

Y1 - 2014

N2 - During DNA replication, nucleosomes are rapidly assembled on newly synthesized DNA to restore chromatin organization. Asf1, a key histone H3-H4 chaperone required for this process, is phosphorylated by Tousled-like kinases (TLKs). Here, we identify TLK phosphorylation sites by mass spectrometry and dissect how phosphorylation has an impact on human Asf1 function. The divergent C-terminal tail of Asf1a is phosphorylated at several sites, and this is required for timely progression through S phase. Consistent with this, biochemical analysis of wild-type and phospho-mimetic Asf1a shows that phosphorylation enhances binding to histones and the downstream chaperones CAF-1 and HIRA. Moreover, we find that TLK phosphorylation of Asf1a is induced in cells experiencing deficiency of new histones and that TLK interaction with Asf1a involves its histone-binding pocket. We thus propose that TLK signalling promotes histone supply in S phase by targeting histone-free Asf1 and stimulating its ability to shuttle histones to sites of chromatin assembly.

AB - During DNA replication, nucleosomes are rapidly assembled on newly synthesized DNA to restore chromatin organization. Asf1, a key histone H3-H4 chaperone required for this process, is phosphorylated by Tousled-like kinases (TLKs). Here, we identify TLK phosphorylation sites by mass spectrometry and dissect how phosphorylation has an impact on human Asf1 function. The divergent C-terminal tail of Asf1a is phosphorylated at several sites, and this is required for timely progression through S phase. Consistent with this, biochemical analysis of wild-type and phospho-mimetic Asf1a shows that phosphorylation enhances binding to histones and the downstream chaperones CAF-1 and HIRA. Moreover, we find that TLK phosphorylation of Asf1a is induced in cells experiencing deficiency of new histones and that TLK interaction with Asf1a involves its histone-binding pocket. We thus propose that TLK signalling promotes histone supply in S phase by targeting histone-free Asf1 and stimulating its ability to shuttle histones to sites of chromatin assembly.

U2 - 10.1038/ncomms4394

DO - 10.1038/ncomms4394

M3 - Journal article

C2 - 24598821

VL - 5

SP - 3394

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -

ID: 104479968