Article
Genetics & Heredity
Emily Biernat, Mansi Verma, Chhabi K. Govind
Summary: RSC is an essential ATP-dependent chromatin remodeling complex in Saccharomyces cerevisiae. It regulates nucleosome-depleted regions (NDRs) by sliding flanking nucleosomes away from NDRs. Depletion of RSC leads to nucleosome encroachment in NDRs and transcription initiation defects. The study compared the effects of catalytic-dead Sth1 and rapid depletion of Sth1 on transcription. Rapid depletion of Sth1 reduces recruitment of TBP and Pol II, while the catalytic-dead mutant exhibits a severe reduction in TBP binding but accumulates Pol II in coding regions. The results suggest a role for RSC in transcription elongation and termination processes.
Article
Cell Biology
Shinya Takahata, Saori Chida, Aoi Ohnuma, Motoyoshi Ando, Takahiro Asanuma, Yota Murakami
Summary: In heterochromatin, Spt16 recruitment is mediated by Pob3 and HP1/Swi6. Pob3 recruits Spt16 through its Spt16 dimerization and PH domains, while HP1/Swi6 recruits Spt16 through physical interaction of the Swi6 CSD and Spt16 peptidase-like domains.
Article
Biochemistry & Molecular Biology
Yue Li, Hongda Huang
Summary: The human facilitates chromatin transcription (FACT) complex, composed of Spt16 and SSRP1, can bind to free H2A-H2B dimer and H3-H4 tetramer (or dimer), as well as partially unraveled nucleosome. The C-terminal domain of human Spt16 (hSpt16-CTD) is crucial for the recognition of H2A-H2B dimer and partially unraveled nucleosome. This study reveals the molecular basis of H2A-H2B dimer recognition by hSpt16-CTD through an acidic intrinsically disordered (AID) segment and identifies some unique structural features of hSpt16-CTD compared to yeast Spt16-CTD. (c) 2023 Elsevier Inc. All rights reserved.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2023)
Article
Biochemistry & Molecular Biology
Barbara Safaric, Erika Chacin, Matthias J. Scherr, Lional Rajappa, Christian Gebhardt, Christoph F. Kurat, Thorben Cordes, Karl E. Duderstadt
Summary: Chromosome replication relies on the recruitment of the nucleosome reorganization activity of the histone chaperone FACT, with coordination from the middle and C-terminal domains of Spt16 and Pob3. The N-terminal region plays a critical role in recruitment by the fork protection complex subunit Tof1. These interactions are essential for robust replication in vitro.
NUCLEIC ACIDS RESEARCH
(2022)
Article
Biochemistry & Molecular Biology
Yu Nakabayashi, Masayuki Seki
Summary: The absence of TBS-III leads to reduced chromatin binding and total amount of centromere proteins, as well as up-regulated transcription at the centromere during M-phase. Ectopic transcription through the centromere displaces key centromere proteins, destabilizing the interaction between centromeres and microtubules, and causing defective chromosome segregation. The identification of new roles for histone binding residues in TBS-III provides new insights into nucleosome function during chromosome segregation.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2022)
Article
Cell Biology
Eutteum Jeong, Jose A. Martina, Pablo S. Contreras, Juhyung Lee, Rosa Puertollano
Summary: TFEB and TFE3 interact with the FACT complex, regulating the transcription of stress-induced genes. FACT plays a crucial role in regulating cellular homeostasis.
Review
Cell Biology
Peijun Wang, Wanting Yang, Shuxin Zhao, Buhe Nashun
Summary: This article discusses the important role of the histone chaperone facilitates chromatin transcription (FACT) in the cell cycle, analyzing its structural characteristics and functions. It explores how FACT regulates chromatin reorganization and its potential roles in transcription, replication, DNA repair, and even cell fate determination.
Article
Plant Sciences
Jiabing Wu, Yue Yang, Jiachen Wang, Youchao Wang, Liufan Yin, Zengxuan An, Kangxi Du, Yan Zhu, Ji Qi, Wen-Hui Shen, Aiwu Dong
Summary: In Arabidopsis, AtChz1A and AtChz1B are histone chaperones that bind to H2A.Z-H2B and facilitate nucleosome assembly. They interact with SWR1 subunit ARP6 and play critical roles in the deposition of H2A.Z, thereby regulating the transcription of genes involved in flowering and other processes.
Article
Cell Biology
Micah J. McCauley, Michael Morse, Nicole Becker, Qi Hu, Maria Victoria Botuyan, Emily Navarrete, Ran Huo, Uma M. Muthurajan, Ioulia Rouzina, Karolin Luger, Georges Mer, James Maher, Mark C. Williams
Summary: The histone chaperone FACT enhances transcription by targeting DNA-protein interactions. This study demonstrates the impact of FACT on nucleosome stability and dynamics, revealing contradictory functions of different FACT subdomains in nucleosome remodeling. These findings provide insights into the catalytic role of key FACT domains in nucleosome disassembly and reassembly.
Article
Cell Biology
Linchang Dai, Xue Xiao, Lu Pan, Liuxin Shi, Ning Xu, Zhuqiang Zhang, Xiaoli Feng, Lu Ma, Shuoxing Dou, Pengye Wang, Bing Zhu, Wei Li, Zheng Zhou
Summary: The study revealed that the N-terminal 1-135 residues of yeast SWR1 complex protein 2 and Swc2-ZN residues play crucial roles in the disassembly/reassembly process of H2A nucleosomes. These residues facilitate the disassembly of H2A nucleosomes and function in the SWR1-catalyzed replacement of H2A with H2A.Z.
Article
Biology
David C. Klein, Santana M. Lardo, Kurtis N. McCannell, Sarah J. Hainer
Summary: The FACT complex maintains cellular pluripotency by regulating nucleosome positioning and transcription activity. FACT interacts with genes such as OCT4, SOX2, and NANOG, binding to both promoter and enhancer elements, and regulates their transcription and expression, thereby influencing cell fate decisions.
Article
Plant Sciences
Aiqing Sun, Chunmei Yin, Min Ma, Ying Zhou, Xiaoyun Zheng, Xiaoyu Tu, Yuda Fang
Summary: This study reveals the involvement of the histone variant H2A.Z in the regulation of plant growth through auxin signaling. It shows that auxin promotes the eviction of H2A.Z from auxin-responsive genes, activating their transcription and influencing plant growth.
Article
Cell Biology
Isabelle Trier, Elizabeth M. Black, Yoon Ki Joo, Lilian Kabeche
Summary: We have found that ATR kinase, a master regulator of the DNA damage response, protects CENP-A protein occupancy at centromeres during interphase independent of DNA damage. Furthermore, ATR-dependent phosphorylation of DAXX protein regulates CENP-A occupancy at centromeres and DAXX localization. Lastly, acute ATR inhibition during interphase leads to kinetochore formation defects and an increased rate of lagging chromosomes. These findings highlight a mechanism by which ATR protects centromere identity and genome stability.
Article
Multidisciplinary Sciences
Marta Barrientos-Moreno, Douglas Maya-Miles, Marina Murillo-Pineda, Sara Fontalva, Monica Perez-Alegre, Eloisa Andujar, Felix Prado
Summary: Genome duplication occurs through the coordinated action of DNA replication and nucleosome assembly. Defective nucleosome assembly causes DNA lesions and loss of chromatin integrity, which can be restored. The mechanism of chromatin restoration is unknown.
SCIENTIFIC REPORTS
(2023)
Article
Cell Biology
Prashant K. Mishra, Henry Wood, John Stanton, Wei-Chun Au, Jessica R. Eisenstatt, Lars Boeckmann, Robert A. Sclafani, Michael Weinreich, Kerry S. Bloom, Peter H. Thorpe, Munira A. Basrai
Summary: The study demonstrates the importance of Cdc7-mediated phosphorylation of Cse4 in faithful chromosome segregation. The regulation of kinetochore proteins by phosphorylation affects cell survival and the accuracy of chromosome segregation.
MOLECULAR BIOLOGY OF THE CELL
(2021)
