| Structural highlights
2ygv is a 8 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Related: | 1fhr, 1j4p, 1k3j, 1k3q, 2hue, 2a0t, 1fhq, 1roc, 1g6g, 1k2n, 1dmz, 1j4o, 1qu5, 1j4l, 1k3n, 1k2m, 1j4q, 1j4k, 1g3g |
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[ASF1_YEAST] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [RAD53_YEAST] Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.[40] [41] [42] [43] [44]
Publication Abstract from PubMed
The histone chaperone Asf1 and the checkpoint kinase Rad53 are found in a complex in budding yeast cells in the absence of genotoxic stress. Our data suggest that this complex involves at least three interaction sites. One site involves the H3-binding surface of Asf11 with an as yet undefined surface of Rad53. A second site is formed by the Rad53-FHA1 domain binding to Asf1-T(270) phosphorylated by casein kinase II. The third site involves the C-terminal 21 amino acids of Rad53 bound to the conserved Asf1 N-terminal domain. The structure of this site showed that the Rad53 C-terminus binds Asf1 in a remarkably similar manner to peptides derived from the histone cochaperones HirA and CAF-I. We call this binding motif, (R/K)R(I/A/V) (L/P), the AIP box for Asf1-Interacting Protein box. Furthermore, C-terminal Rad53-F(820) binds the same pocket of Asf1 as does histone H4-F(100). Thus Rad53 competes with histones H3-H4 and cochaperones HirA/CAF-I for binding to Asf1. Rad53 is phosphorylated and activated upon genotoxic stress. The Asf1-Rad53 complex dissociated when cells were treated with hydroxyurea but not methyl-methane-sulfonate, suggesting a regulation of the complex as a function of the stress. We identified a rad53 mutation that destabilized the Asf1-Rad53 complex and increased the viability of rad9 and rad24 mutants in conditions of genotoxic stress, suggesting that complex stability impacts the DNA damage response.
Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction.,Jiao Y, Seeger K, Lautrette A, Gaubert A, Mousson F, Guerois R, Mann C, Ochsenbein F Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2866-71. Epub 2012 Feb 9. PMID:22323608[45]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
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- ↑ Green EM, Antczak AJ, Bailey AO, Franco AA, Wu KJ, Yates JR 3rd, Kaufman PD. Replication-independent histone deposition by the HIR complex and Asf1. Curr Biol. 2005 Nov 22;15(22):2044-9. PMID:16303565 doi:http://dx.doi.org/S0960-9822(05)01306-0
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- ↑ Linger J, Tyler JK. The yeast histone chaperone chromatin assembly factor 1 protects against double-strand DNA-damaging agents. Genetics. 2005 Dec;171(4):1513-22. Epub 2005 Sep 2. PMID:16143623 doi:http://dx.doi.org/genetics.105.043000
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- ↑ Zabaronick SR, Tyler JK. The histone chaperone anti-silencing function 1 is a global regulator of transcription independent of passage through S phase. Mol Cell Biol. 2005 Jan;25(2):652-60. PMID:15632066 doi:http://dx.doi.org/25/2/652
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- ↑ Lewis LK, Karthikeyan G, Cassiano J, Resnick MA. Reduction of nucleosome assembly during new DNA synthesis impairs both major pathways of double-strand break repair. Nucleic Acids Res. 2005 Sep 1;33(15):4928-39. Print 2005. PMID:16141196 doi:http://dx.doi.org/33/15/4928
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- ↑ Tamburini BA, Carson JJ, Linger JG, Tyler JK. Dominant mutants of the Saccharomyces cerevisiae ASF1 histone chaperone bypass the need for CAF-1 in transcriptional silencing by altering histone and Sir protein recruitment. Genetics. 2006 Jun;173(2):599-610. Epub 2006 Apr 2. PMID:16582440 doi:http://dx.doi.org/10.1534/genetics.105.054783
- ↑ Korber P, Barbaric S, Luckenbach T, Schmid A, Schermer UJ, Blaschke D, Horz W. The histone chaperone Asf1 increases the rate of histone eviction at the yeast PHO5 and PHO8 promoters. J Biol Chem. 2006 Mar 3;281(9):5539-45. Epub 2006 Jan 4. PMID:16407267 doi:http://dx.doi.org/M513340200
- ↑ Schneider J, Bajwa P, Johnson FC, Bhaumik SR, Shilatifard A. Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J Biol Chem. 2006 Dec 8;281(49):37270-4. Epub 2006 Oct 17. PMID:17046836 doi:http://dx.doi.org/10.1074/jbc.C600265200
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- ↑ Kats ES, Albuquerque CP, Zhou H, Kolodner RD. Checkpoint functions are required for normal S-phase progression in Saccharomyces cerevisiae RCAF- and CAF-I-defective mutants. Proc Natl Acad Sci U S A. 2006 Mar 7;103(10):3710-5. Epub 2006 Feb 24. PMID:16501045 doi:http://dx.doi.org/0511102103
- ↑ Recht J, Tsubota T, Tanny JC, Diaz RL, Berger JM, Zhang X, Garcia BA, Shabanowitz J, Burlingame AL, Hunt DF, Kaufman PD, Allis CD. Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6988-93. Epub 2006 Apr 20. PMID:16627621 doi:http://dx.doi.org/0601676103
- ↑ Adkins MW, Carson JJ, English CM, Ramey CJ, Tyler JK. The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase. J Biol Chem. 2007 Jan 12;282(2):1334-40. Epub 2006 Nov 15. PMID:17107956 doi:http://dx.doi.org/M608025200
- ↑ Tsubota T, Berndsen CE, Erkmann JA, Smith CL, Yang L, Freitas MA, Denu JM, Kaufman PD. Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell. 2007 Mar 9;25(5):703-12. Epub 2007 Feb 22. PMID:17320445 doi:S1097-2765(07)00086-X
- ↑ Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD. Structure and function of the conserved core of histone deposition protein Asf1. Curr Biol. 2003 Dec 16;13(24):2148-58. PMID:14680630
- ↑ Zheng P, Fay DS, Burton J, Xiao H, Pinkham JL, Stern DF. SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase. Mol Cell Biol. 1993 Sep;13(9):5829-42. PMID:8355715
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- ↑ Sanchez Y, Bachant J, Wang H, Hu F, Liu D, Tetzlaff M, Elledge SJ. Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms. Science. 1999 Nov 5;286(5442):1166-71. PMID:10550056
- ↑ Kim EM, Jang YK, Park SD. Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. Nucleic Acids Res. 2002 Feb 1;30(3):643-8. PMID:11809875
- ↑ Pike BL, Yongkiettrakul S, Tsai MD, Heierhorst J. Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae. Mol Cell Biol. 2004 Apr;24(7):2779-88. PMID:15024067
- ↑ Jiao Y, Seeger K, Lautrette A, Gaubert A, Mousson F, Guerois R, Mann C, Ochsenbein F. Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction. Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2866-71. Epub 2012 Feb 9. PMID:22323608 doi:10.1073/pnas.1106023109
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