Histone Deacetylases: Transcriptional Regulation and Other by ERIC VERDIN PDF


ISBN-10: 1588294994

ISBN-13: 9781588294999

A panel of prime investigators summarizes and synthesizes the hot discoveries within the quickly evolving box of histone acetylation as a key regulatory mechanism for gene expression. The authors describe what has been realized approximately those proteins, together with the id of the enzymes, the elucidation of the enzymatic mechanisms of motion, and the id in their substrates and their companions. additionally they overview the buildings which were solved for a couple of enzymes-both on my own and in advanced with small molecule inhibitors-and the organic roles of the different histone deacetylases (HDAC) genes which have been knocked out in mice.

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Additional info for Histone Deacetylases: Transcriptional Regulation and Other Cellular Functions (Cancer Drug Discovery and Development)

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Curr Opin Cell Biol 2003;15:164–171. 53. Ito A, Kawaguchi Y, Lai CH, et al. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J 2002;21:6236–6245. 54. Luo J, Li M, Tang Y, Laszkowska M, Roeder RG, Gu W. Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo. Proc Natl Acad Sci U S A 2004;101:2259–2264. 55. Privalsky ML. The role of corepressors in transcriptional regulation by nuclear hormone receptors. Annu Rev Physiol 2004;66:315–360. 56.

For abbreviations, see Acronyms and Abbreviations table. See Color Plate 3 following p. 180. PYR. PYR is a SWI/SNF-related complex that binds to DNA containing pyrimidine-rich sequences located between the human fetal and adult β-globin-like genes (81). Interestingly, this DNA binding activity is specific to adult hematopoietic cells. The complex contains the lymphocyte-specific transcription factor Ikaros, the NuRD core complex except for HDAC1, and at least five SWI/SNF complex-related proteins—Brg1, Baf57, Baf60a, Srg3, Ini1, and Baf170 (82).

Its main feature is the presence of an HMG domain that confers an ability to bind DNA, which is critical for the repressive activity of the CoREST complex in vivo (85). There is not much known about BHC80, except that it contains one PHD and two leucine zipper domains (85,93), all of which are involved in protein–protein interactions. However, in contrast to the ubiquitous BRAF35, the presence of BHC80 is highly tissue specific, perhaps reflective of a specialized role (85,93). Interestingly, a supracomplex that contains the CoREST complex was isolated through affinity purification of the corepressor CtBP (94,95).

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Histone Deacetylases: Transcriptional Regulation and Other Cellular Functions (Cancer Drug Discovery and Development) by ERIC VERDIN

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