5u2j

MORF double PHD finger (DPF) in complex with histone H3K14buMORF double PHD finger (DPF) in complex with histone H3K14bu

Structural highlights

5u2j is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Activity:	Histone acetyltransferase, with EC number 2.3.1.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[KAT6B_HUMAN] Genitopatellar syndrome;Noonan syndrome;Blepharophimosis-intellectual disability syndrome, SBBYS type. A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP.^[1] The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[KAT6B_HUMAN] Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.^[2] ^[3] ^[4]

Publication Abstract from PubMed

The monocytic leukemia zinc-finger protein-related factor (MORF) is a transcriptional coactivator and a catalytic subunit of the lysine acetyltransferase complex implicated in cancer and developmental diseases. We have previously shown that the double plant homeodomain finger (DPF) of MORF is capable of binding to acetylated histone H3. Here we demonstrate that the DPF of MORF recognizes many newly identified acylation marks. The mass spectrometry study provides comprehensive analysis of H3K14 acylation states in vitro and in vivo. The crystal structure of the MORF DPF-H3K14butyryl complex offers insight into the selectivity of this reader toward lipophilic acyllysine substrates. Together, our findings support the mechanism by which the acetyltransferase MORF promotes spreading of histone acylation.

Recognition of Histone H3K14 Acylation by MORF.,Klein BJ, Simithy J, Wang X, Ahn J, Andrews FH, Zhang Y, Cote J, Shi X, Garcia BA, Kutateladze TG Structure. 2017 Apr 4;25(4):650-654.e2. doi: 10.1016/j.str.2017.02.003. Epub 2017, Mar 9. PMID:28286003^[5]

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

References

↑ Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B. Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. PMID:11157802
↑ Champagne N, Bertos NR, Pelletier N, Wang AH, Vezmar M, Yang Y, Heng HH, Yang XJ. Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein. J Biol Chem. 1999 Oct 1;274(40):28528-36. PMID:10497217
↑ Pelletier N, Champagne N, Stifani S, Yang XJ. MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. Oncogene. 2002 Apr 18;21(17):2729-40. PMID:11965546 doi:10.1038/sj.onc.1205367
↑ Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007
↑ Klein BJ, Simithy J, Wang X, Ahn J, Andrews FH, Zhang Y, Cote J, Shi X, Garcia BA, Kutateladze TG. Recognition of Histone H3K14 Acylation by MORF. Structure. 2017 Apr 4;25(4):650-654.e2. doi: 10.1016/j.str.2017.02.003. Epub 2017, Mar 9. PMID:28286003 doi:http://dx.doi.org/10.1016/j.str.2017.02.003

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OCA

[1] Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B. Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. PMID:11157802

[2] Champagne N, Bertos NR, Pelletier N, Wang AH, Vezmar M, Yang Y, Heng HH, Yang XJ. Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein. J Biol Chem. 1999 Oct 1;274(40):28528-36. PMID:10497217

[3] Pelletier N, Champagne N, Stifani S, Yang XJ. MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. Oncogene. 2002 Apr 18;21(17):2729-40. PMID:11965546 doi:10.1038/sj.onc.1205367

[4] Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007

[5] Klein BJ, Simithy J, Wang X, Ahn J, Andrews FH, Zhang Y, Cote J, Shi X, Garcia BA, Kutateladze TG. Recognition of Histone H3K14 Acylation by MORF. Structure. 2017 Apr 4;25(4):650-654.e2. doi: 10.1016/j.str.2017.02.003. Epub 2017, Mar 9. PMID:28286003 doi:http://dx.doi.org/10.1016/j.str.2017.02.003

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