The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation
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1. | Title | Title of document | The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation |
2. | Creator | Author's name, affiliation, country | N. V. Soshnikova; Institute of Gene Biology Russian Academy of Sciences; Россия |
2. | Creator | Author's name, affiliation, country | A. A. Sheynov; Institute of Gene Biology Russian Academy of Sciences; Россия |
2. | Creator | Author's name, affiliation, country | Eu. V. Tatarskiy; Institute of Gene Biology Russian Academy of Sciences; Россия |
2. | Creator | Author's name, affiliation, country | S. G. Georgieva; Institute of Gene Biology Russian Academy of Sciences; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences; Россия |
3. | Subject | Discipline(s) | |
3. | Subject | Keyword(s) | DPF domains; tandem PHD; MOZ and MORF histone acetyltransferases; DPF1; DPF2; DPF3; PHF10; BAF; PBAF |
4. | Description | Abstract | The DPF (double PHD finger) domain consists of two PHD fingers organized in tandem. The two PHD-finger domains within a DPF form a single structure that interacts with the modification of the N-terminal histone fragment in a way different from that for single PHD fingers. Several histone modifications interacting with the DPF domain have already been identified. They include acetylation of H3K14 and H3K9, as well as crotonylation of H3K14. These modifications are found predominantly in transcriptionally active chromatin. Proteins containing DPF belong to two classes of protein complexes, which are the transcriptional coactivators involved in the regulation of the chromatin structure. These are the histone acetyltransferase complex belonging to the MYST family and the SWI/SNF chromatin-remodeling complex. The DPF domain is responsible for the specificity of the interactions between these complexes and chromatin. Proteins containing DPF play a crucial role in the activation of the transcription of a number of genes expressed during the development of an organism. These genes are important in the differentiation and malignant transformation of mammalian cells. |
5. | Publisher | Organizing agency, location | Acta Naturae Ltd |
6. | Contributor | Sponsor(s) |
Russian Science Foundation (18-14-00303) |
7. | Date | (DD-MM-YYYY) | 22.12.2020 |
8. | Type | Status & genre | Peer-reviewed Article |
8. | Type | Type | Review Article |
9. | Format | File format | |
10. | Identifier | Uniform Resource Identifier | https://actanaturae.ru/2075-8251/article/view/11092 |
10. | Identifier | Digital Object Identifier (DOI) | 10.32607/actanaturae.11092 |
11. | Source | Title; vol., no. (year) | Acta Naturae; Vol 12, No 4 (2020) |
12. | Language | English=en | ru |
13. | Relation | Supp. Files |
Fig. 1. Proteins and complexes containing the DPF domains. (A) – Domain organization of the MOZ, MORF, DPF1, DPF2, DPF3b, and PHF10-P proteins. The DPF domains are shown with blue boxes. (B) – Schematic representation of the complexes containing the corresponding proteins with the DPF domains: histone acetyltransferase MYST-family HAT complex; BAF and PBAF chromatin remodeling complexes (427KB) doi: 10.32607/20758251-2020-12-4-57-65-1681 Fig. 2. Alignment of the amino acid sequences of the DPF motifs of the MOZ, MORF, DPF1, DPF2, DPF3b, and PHF10-P human proteins. Schematic representation of the secondary structures of PHD1 and PHD2 is shown above the sequences. Cysteine and histidine residues coordinating Zn ions in PHD1 and PHD2 are indicated in blue and green, respectively. Homologous amino acids in PHD1 that form a hydrophobic pocket and bind H3K14ac/cr are highlighted in blue. Homologous amino acids that form an acidic pocket and bind to the first to fourth N-terminal amino acids of histone H3 are highlighted in green (322KB) doi: 10.32607/20758251-2020-12-4-57-65-1683 Fig. 3. Schematic representation of the activities of the MYST-family HAT (A) and BAF (B) complexes containing either the MOZ/MORF or DPF1-3 protein. The interaction between the DPF domains and histone modifications (black arrows), as well as the histone acetyltransferase activity of the MYST complex (gray arrows) (A) and the chromatin remodeling activity of the BAF complex (blue arrow) (B), is shown (341KB) doi: 10.32607/20758251-2020-12-4-57-65-1685 |
14. | Coverage | Geo-spatial location, chronological period, research sample (gender, age, etc.) | |
15. | Rights | Copyright and permissions |
Copyright (c) 2020 Soshnikova N.V., Sheynov A.A., Tatarskiy E.V., Georgieva S.G.![]() This work is licensed under a Creative Commons Attribution 4.0 International License. |