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Poster Session : The role of histone H3 K4 methyltransferase, Set1p, in global chromatin maintenance
( Ja Hwan Seol ),( Hye Jin Kim ),( Young Jin Yang ),( Jae Hyun Yang ),( Da Hee Lee ),( Jeong Whan Han ),( Hyang Woo Lee ),( Eun Jung Cho ) 한국생화학분자생물학회 (구 한국생화학회) 2006 생화학분자생물학회 춘계학술발표논문집 Vol.2006 No.-
Song, Yunkyoung,Seol, Ja-Hwan,Yang, Jae-Hyun,Kim, Hye-Jin,Han, Jeung-Whan,Youn, Hong-Duk,Cho, Eun-Jung Oxford University Press 2013 Nucleic acids research Vol.41 No.10
<P>The mammalian genome encodes multiple variants of histone H3 including H3.1/H3.2 and H3.3. In contrast to H3.1/H3.2, H3.3 is enriched in the actively transcribed euchromatin and the telomeric heterochromatins. However, the mechanism for H3.3 to incorporate into the different domains of chromatin is not known. Here, taking the advantage of well-defined transcription analysis system of yeast, we attempted to understand the molecular mechanism of selective deposition of human H3.3 into actively transcribed genes. We show that there are systemic H3 substrate-selection mechanisms operating even in yeasts, which encode a single type of H3. Yeast HIR complex mediated H3-specific recognition specificity for deposition of H3.3 in the transcribed genes. A critical component of this process was the H3 A-IG code composed of amino acids 87, 89 and 90. The preference toward H3.3 was completely lost when HIR subunits were absent and partially suppressed by human HIRA. Asf1 allows the influx of H3, regardless of H3 type. We propose that H3.3 is introduced into the active euchromatin by targeting the recycling pathway that is mediated by HIRA (or HIR), and this H3-selection mechanism is highly conserved through the evolution. These results also uncover an unexpected role of RI chaperones in evolution of variant H3s.</P>
Myogenic transcriptional activation of MyoD mediated by replication-independent histone deposition.
Yang, Jae-Hyun,Song, Yunkyoung,Seol, Ja-Hwan,Park, Jin Young,Yang, Yong-Jin,Han, Jeung-Whan,Youn, Hong-Duk,Cho, Eun-Jung National Academy of Sciences 2011 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.108 No.1
<P>In mammals, the canonical histone H3 and the variant H3.3 are assembled into chromatin through replication-coupled and replication-independent (RI) histone deposition pathways, respectively, to play distinct roles in chromatin function. H3.3 is largely associated with transcriptionally active regions via the activity of RI histone chaperone, HIRA. However, the precise role of the RI pathway and HIRA in active transcription and the mechanisms by which H3.3 affects gene activity are not known. In this study, we show that HIRA is an essential factor for muscle development by establishing MyoD activation in myotubes. HIRA and Asf1a, but not CHD1 or Asf1b, mediate H3.3 incorporation in the promoter and the critical upstream regulatory regions of the MyoD gene. HIRA and H3.3 are required for epigenetic transition into the more permissive chromatin structure for polymerase II recruitment to the promoter, regardless of transcription-associated covalent modification of histones. Our results suggest distinct epigenetic management of the master regulator with RI pathway components for cellular differentiation.</P>
Role of RNA Polymerase II Carboxy Terminal Domain Phosphorylation in DNA Damage Response
Jeong Su-Jin,Kim Hye-Jin,Yang Yong-Jin,Seol Ja-Hwan,Jung Bo-Young,Han Jeong-Whan,Lee Hyang-Woo,Cho Eun-Jung The Microbiological Society of Korea 2005 The journal of microbiology Vol.43 No.6
The phosphorylation of C-terminal domain (CTD) of Rpb1p, the largest subunit of RNA polymerase II plays an important role in transcription and the coupling of various cellular events to transcription. In this study, its role in DNA damage response is closely examined in Saccharomyces cerevisiae, focusing specifically on several transcription factors that mediate or respond to the phosphorylation of the CTD. CTDK-1, the pol II CTD kinase, FCP1, the CTD phosphatase, ESS1, the CTD phosphorylation dependent cis-trans isomerase, and RSP5, the phosphorylation dependent pol II ubiquitinating enzyme, were chosen for the study. We determined that the CTD phosphorylation of CTD, which occurred predominantly at serine 2 within a heptapeptide repeat, was enhanced in response to a variety of sources of DNA damage. This modification was shown to be mediated by CTDK-1. Although mutations in ESS1 or FCP1 caused cells to become quite sensitive to DNA damage, the characteristic pattern of CTD phosphorylation remained unaltered, thereby implying that ESS1 and FCP1 play roles downstream of CTD phosphorylation in response to DNA damage. Our data suggest that the location or extent of CTD phosphorylation might be altered in response to DNA damage, and that the modified CTD, ESS1, and FCP1 all contribute to cellular survival in such conditions.