| Structural highlights
Function
[KAT5_HUMAN] Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10]
Publication Abstract from PubMed
Tat-interactive protein 60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and nonhistone proteins in diverse cellular processes. While TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here, we attempted a quantitative analysis of the interaction between the human TIP60-CB and histone peptides, but did not observe any detectable binding by either fluorescence polarization or isothermal titration calorimetry assays. We also determined the crystal structure of the TIP60-CB alone. Analysis of the apo-structure reveals a putative peptide-binding site that might be occluded by the basic side chain of a residue in a unique beta hairpin between the two N-terminal strands of the beta barrel, leading to the inability of TIP60-CB to bind histones.
Structural and histone binding studies of the chromo barrel domain of TIP60.,Zhang Y, Lei M, Yang X, Feng Y, Yang Y, Loppnau P, Li Y, Yang Y, Min J, Liu Y FEBS Lett. 2018 Apr;592(7):1221-1232. doi: 10.1002/1873-3468.13021. Epub 2018 Mar, 25. PMID:29494751[11]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, Chan HM, Livingston DM, Amati B. MYC recruits the TIP60 histone acetyltransferase complex to chromatin. EMBO Rep. 2003 Jun;4(6):575-80. PMID:12776177 doi:http://dx.doi.org/10.1038/sj.embor.embor861
- ↑ Legube G, Linares LK, Tyteca S, Caron C, Scheffner M, Chevillard-Briet M, Trouche D. Role of the histone acetyl transferase Tip60 in the p53 pathway. J Biol Chem. 2004 Oct 22;279(43):44825-33. Epub 2004 Aug 13. PMID:15310756 doi:http://dx.doi.org/10.1074/jbc.M407478200
- ↑ Doyon Y, Selleck W, Lane WS, Tan S, Cote J. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. PMID:14966270
- ↑ Taubert S, Gorrini C, Frank SR, Parisi T, Fuchs M, Chan HM, Livingston DM, Amati B. E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1. Mol Cell Biol. 2004 May;24(10):4546-56. PMID:15121871
- ↑ Berns K, Hijmans EM, Mullenders J, Brummelkamp TR, Velds A, Heimerikx M, Kerkhoven RM, Madiredjo M, Nijkamp W, Weigelt B, Agami R, Ge W, Cavet G, Linsley PS, Beijersbergen RL, Bernards R. A large-scale RNAi screen in human cells identifies new components of the p53 pathway. Nature. 2004 Mar 25;428(6981):431-7. PMID:15042092 doi:http://dx.doi.org/10.1038/nature02371
- ↑ Sun Y, Jiang X, Chen S, Fernandes N, Price BD. A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13182-7. Epub 2005 Sep 2. PMID:16141325 doi:http://dx.doi.org/0504211102
- ↑ 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
- ↑ Wang J, Liu N, Liu Z, Li Y, Song C, Yuan H, Li YY, Zhao X, Lu H. The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter. Biochim Biophys Acta. 2008 Feb;1783(2):224-36. Epub 2007 Oct 4. PMID:17996965 doi:http://dx.doi.org/10.1016/j.bbamcr.2007.09.004
- ↑ Kikuchi M, Okumura F, Tsukiyama T, Watanabe M, Miyajima N, Tanaka J, Imamura M, Hatakeyama S. TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells. Biochim Biophys Acta. 2009 Dec;1793(12):1828-36. doi:, 10.1016/j.bbamcr.2009.11.001. Epub 2009 Nov 10. PMID:19909775 doi:http://dx.doi.org/10.1016/j.bbamcr.2009.11.001
- ↑ Obri A, Ouararhni K, Papin C, Diebold ML, Padmanabhan K, Marek M, Stoll I, Roy L, Reilly PT, Mak TW, Dimitrov S, Romier C, Hamiche A. ANP32E is a histone chaperone that removes H2A.Z from chromatin. Nature. 2014 Jan 30;505(7485):648-53. doi: 10.1038/nature12922. Epub 2014 Jan 22. PMID:24463511 doi:http://dx.doi.org/10.1038/nature12922
- ↑ Zhang Y, Lei M, Yang X, Feng Y, Yang Y, Loppnau P, Li Y, Yang Y, Min J, Liu Y. Structural and histone binding studies of the chromo barrel domain of TIP60. FEBS Lett. 2018 Apr;592(7):1221-1232. doi: 10.1002/1873-3468.13021. Epub 2018 Mar, 25. PMID:29494751 doi:http://dx.doi.org/10.1002/1873-3468.13021
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