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Article

JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions

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Institute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany
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Institute for Biochemistry, Justus-Liebig-University Giessen, 35392 Giessen, Germany
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Department of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany
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Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
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Genomics Core Facility, Institute of Molecular Oncology, Member of the German Center for Lung Research (DZL), Philipps-University Marburg, 35043 Marburg, Germany
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Biomedical Informatics and Systems Medicine, Justus-Liebig-University Giessen, 35392 Giessen, Germany
*
Authors to whom correspondence should be addressed.
Current Address: Sandoz/Hexal AG, 83607 Holzkirchen, Germany.
Current Address: Department of DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
§
Current Address: Vertex Pharmaceuticals, 80331 Munich, Germany.
Current Address: Cellzome GmbH, a GSK company, 69117 Heidelberg, Germany.
Int. J. Mol. Sci. 2021, 22(2), 678; https://doi.org/10.3390/ijms22020678
Received: 21 December 2020 / Revised: 7 January 2021 / Accepted: 9 January 2021 / Published: 12 January 2021
(This article belongs to the Special Issue Positioning of Nucleosomes)
Histone variants differ in amino acid sequence, expression timing and genomic localization sites from canonical histones and convey unique functions to eukaryotic cells. Their tightly controlled spatial and temporal deposition into specific chromatin regions is accomplished by dedicated chaperone and/or remodeling complexes. While quantitatively identifying the chaperone complexes of many human H2A variants by using mass spectrometry, we also found additional members of the known H2A.Z chaperone complexes p400/TIP60/NuA4 and SRCAP. We discovered JAZF1, a nuclear/nucleolar protein, as a member of a p400 sub-complex containing MBTD1 but excluding ANP32E. Depletion of JAZF1 results in transcriptome changes that affect, among other pathways, ribosome biogenesis. To identify the underlying molecular mechanism contributing to JAZF1’s function in gene regulation, we performed genome-wide ChIP-seq analyses. Interestingly, depletion of JAZF1 leads to reduced H2A.Z acetylation levels at > 1000 regulatory sites without affecting H2A.Z nucleosome positioning. Since JAZF1 associates with the histone acetyltransferase TIP60, whose depletion causes a correlated H2A.Z deacetylation of several JAZF1-targeted enhancer regions, we speculate that JAZF1 acts as chromatin modulator by recruiting TIP60’s enzymatic activity. Altogether, this study uncovers JAZF1 as a member of a TIP60-containing p400 chaperone complex orchestrating H2A.Z acetylation at regulatory regions controlling the expression of genes, many of which are involved in ribosome biogenesis. View Full-Text
Keywords: JAZF1; H2A.Z; histone variants; TIP60; acetylation; enhancer; gene regulation; ribosome JAZF1; H2A.Z; histone variants; TIP60; acetylation; enhancer; gene regulation; ribosome
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MDPI and ACS Style

Procida, T.; Friedrich, T.; Jack, A.P.M.; Peritore, M.; Bönisch, C.; Eberl, H.C.; Daus, N.; Kletenkov, K.; Nist, A.; Stiewe, T.; Borggrefe, T.; Mann, M.; Bartkuhn, M.; Hake, S.B. JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions. Int. J. Mol. Sci. 2021, 22, 678. https://doi.org/10.3390/ijms22020678

AMA Style

Procida T, Friedrich T, Jack APM, Peritore M, Bönisch C, Eberl HC, Daus N, Kletenkov K, Nist A, Stiewe T, Borggrefe T, Mann M, Bartkuhn M, Hake SB. JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions. International Journal of Molecular Sciences. 2021; 22(2):678. https://doi.org/10.3390/ijms22020678

Chicago/Turabian Style

Procida, Tara, Tobias Friedrich, Antonia P.M. Jack, Martina Peritore, Clemens Bönisch, H. C. Eberl, Nadine Daus, Konstantin Kletenkov, Andrea Nist, Thorsten Stiewe, Tilman Borggrefe, Matthias Mann, Marek Bartkuhn, and Sandra B. Hake 2021. "JAZF1, A Novel p400/TIP60/NuA4 Complex Member, Regulates H2A.Z Acetylation at Regulatory Regions" International Journal of Molecular Sciences 22, no. 2: 678. https://doi.org/10.3390/ijms22020678

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