3qm0

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Revision as of 16:52, 25 December 2014

Crystal structure of RTT109-AC-CoA complex

Structural highlights

3qm0 is a 1 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 3d35. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	KIM2, L1377, REM50, RTT109, YLL002W (Saccharomyces cerevisiae)
Activity:	Histone acetyltransferase, with EC number 2.3.1.48
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RT109_YEAST] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

Rtt109, also known as KAT11, is a recently characterized fungal-specific histone acetyltransferase (HAT) that modifies histone H3 lysine 56 (H3K56) to promote genome stability. Rtt109 does not show sequence conservation with other known HATs and depends on association with either of two histone chaperones, Asf1 or Vps75, for HAT activity. Here we report the X-ray crystal structure of an Rtt109-acetyl coenzyme A complex and carry out structure-based mutagenesis, combined with in vitro biochemical studies of the Rtt109-Vps75 complex and studies of Rtt109 function in vivo. The Rtt109 structure reveals noteworthy homology to the metazoan p300/CBP HAT domain but exhibits functional divergence, including atypical catalytic properties and mode of cofactor regulation. The structure reveals a buried autoacetylated lysine residue that we show is also acetylated in the Rtt109 protein purified from yeast cells. Implications for understanding histone substrate and chaperone binding by Rtt109 are discussed.

Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.,Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, Gharib M, Jiang E, Thibault P, Verreault A, Cole PA, Marmorstein R Nat Struct Mol Biol. 2008 Jul;15(7):738-45. Epub 2008 Jun 22. PMID:18568037^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Scholes DT, Banerjee M, Bowen B, Curcio MJ. Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics. 2001 Dec;159(4):1449-65. PMID:11779788
↑ 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
↑ Han J, Zhou H, Li Z, Xu RM, Zhang Z. The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3. J Biol Chem. 2007 May 11;282(19):14158-64. Epub 2007 Mar 16. PMID:17369253 doi:http://dx.doi.org/10.1074/jbc.M700611200
↑ Han J, Zhou H, Li Z, Xu RM, Zhang Z. Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J Biol Chem. 2007 Sep 28;282(39):28587-96. Epub 2007 Aug 9. PMID:17690098 doi:http://dx.doi.org/10.1074/jbc.M702496200
↑ 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
↑ Driscoll R, Hudson A, Jackson SP. Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science. 2007 Feb 2;315(5812):649-52. PMID:17272722 doi:http://dx.doi.org/315/5812/649
↑ Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM, Zhang Z. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science. 2007 Feb 2;315(5812):653-5. PMID:17272723 doi:http://dx.doi.org/10.1126/science.1133234
↑ Williams SK, Truong D, Tyler JK. Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc Natl Acad Sci U S A. 2008 Jul 1;105(26):9000-5. doi:, 10.1073/pnas.0800057105. Epub 2008 Jun 24. PMID:18577595 doi:http://dx.doi.org/10.1073/pnas.0800057105
↑ Tang Y, Meeth K, Jiang E, Luo C, Marmorstein R. Structure of Vps75 and implications for histone chaperone function. Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12206-11. Epub 2008 Aug 22. PMID:18723682
↑ Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, Gharib M, Jiang E, Thibault P, Verreault A, Cole PA, Marmorstein R. Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Nat Struct Mol Biol. 2008 Jul;15(7):738-45. Epub 2008 Jun 22. PMID:18568037 doi:10.1038/nsmb.1448

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3qm0"

@@ Line 9: / Line 9: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qm0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qm0 RCSB], [http://www.ebi.ac.uk/pdbsum/3qm0 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RT109_YEAST RT109_YEAST]] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:17046836</ref> <ref>PMID:17369253</ref> <ref>PMID:17690098</ref> <ref>PMID:17320445</ref> <ref>PMID:17272722</ref> <ref>PMID:17272723</ref> <ref>PMID:18577595</ref> <ref>PMID:18723682</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==