Cargando…

Transient Kinetic Analysis of SWR1C-Catalyzed H2A.Z Deposition Unravels the Impact of Nucleosome Dynamics and the Asymmetry of Histone Exchange

The SWR1C chromatin remodeling enzyme catalyzes ATP-dependent replacement of nucleosomal H2A with the H2A.Z variant, regulating key DNA-mediated processes such as transcription and DNA repair. Here, we investigate the transient kinetic mechanism of the histone exchange reaction, employing ensemble F...

Descripción completa

Detalles Bibliográficos
Autores principales:	Singh, Raushan K., Fan, Jiayl, Gioacchini, Nathan, Watanabe, Shinya, Bilsel, Osman, Peterson, Craig L.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	2019
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6545893/ https://www.ncbi.nlm.nih.gov/pubmed/30970243 http://dx.doi.org/10.1016/j.celrep.2019.03.035

Ejemplares similares

Dual engagement of the nucleosomal acidic patches is essential for deposition of histone H2A.Z by SWR1C
por: Baier, Alexander S., et al.
Publicado: (2023)

H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast
por: Ranjan, Anand, et al.
Publicado: (2015)

Functional characterization and architecture of recombinant yeast SWR1 histone exchange complex
por: Lin, Chia-Liang, et al.
Publicado: (2017)

H2A.Z deposition by SWR1C involves multiple ATP-dependent steps
por: Fan, Jiayi, et al.
Publicado: (2022)

The SWR1 Histone Replacement Complex Causes Genetic Instability and Genome-Wide Transcription Misregulation in the Absence of H2A.Z
por: Morillo-Huesca, Macarena, et al.
Publicado: (2010)

Arabidopsis SWR1-associated protein methyl-CpG-binding domain 9 is required for histone H2A.Z deposition
por: Potok, Magdalena E., et al.
Publicado: (2019)

Spontaneous histone exchange between nucleosomes
por: Das, Subhra Kanti, et al.
Publicado: (2023)

Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A
por: Choi, Jongkyu, et al.
Publicado: (2009)

SWR1-Independent Association of H2A.Z to the LINC Complex Promotes Meiotic Chromosome Motion
por: González-Arranz, Sara, et al.
Publicado: (2020)

Histone variant H2A.Z modulates nucleosome dynamics to promote DNA accessibility
por: Li, Shuxiang, et al.
Publicado: (2023)

H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilization
por: Bönisch, Clemens, et al.
Publicado: (2012)

A Protein Complex Containing the Conserved Swi2/Snf2-Related ATPase Swr1p Deposits Histone Variant H2A.Z into Euchromatin
por: Kobor, Michael. S, et al.
Publicado: (2004)

Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A
por: Horikoshi, Naoki, et al.
Publicado: (2016)

Coordinated DNA and histone dynamics drive accurate histone H2A.Z exchange
por: Poyton, Matthew F., et al.
Publicado: (2022)

Structural analyses of the chromatin remodeling enzymes INO80-C and SWR-C
por: Watanabe, Shinya, et al.
Publicado: (2015)

Histone variant H2A.Z regulates nucleosome unwrapping and CTCF binding in mouse ES cells
por: Wen, Zengqi, et al.
Publicado: (2020)

The histone variant H2A.Z in yeast is almost exclusively incorporated into the +1 nucleosome in the direction of transcription
por: Bagchi, Dia N, et al.
Publicado: (2020)

Asymmetry in histone rotation in forced unwrapping and force quench rewrapping in a nucleosome
por: Reddy, Govardhan, et al.
Publicado: (2021)

The Histone Variant H2A.Z C-Terminal Domain Has Locus-Specific Differential Effects on H2A.Z Occupancy and Nucleosome Localization
por: Neumann, Hannah, et al.
Publicado: (2023)

SWR1 Chromatin-Remodeling Complex Subunits and H2A.Z Have Non-overlapping Functions in Immunity and Gene Regulation in Arabidopsis
por: Berriri, Souha, et al.
Publicado: (2016)

Variant Histone H2A.Z Is Globally Localized to the Promoters of Inactive Yeast Genes and Regulates Nucleosome Positioning
por: Guillemette, Benoît, et al.
Publicado: (2005)

Discriminating nucleosomes containing histone H2A.Z or H2A based on genetic and epigenetic information
por: Gervais, Alain L, et al.
Publicado: (2009)

The N‐terminal and C‐terminal halves of histone H2A.Z independently function in nucleosome positioning and stability
por: Sato, Shoko, et al.
Publicado: (2020)

Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction
por: Sun, Lu, et al.
Publicado: (2017)

DNA-dependent protein kinase catalytic subunit (DNA-PKcs) contributes to incorporation of histone variant H2A.Z into nucleosomes
por: Wang, Ling-Yao, et al.
Publicado: (2019)

Podbat: A Novel Genomic Tool Reveals Swr1-Independent H2A.Z Incorporation at Gene Coding Sequences through Epigenetic Meta-Analysis
por: Sadeghi, Laia, et al.
Publicado: (2011)

Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
por: Elliott, Giles O., et al.
Publicado: (2013)

H2A.Z nucleosomes enriched over active genes are homotypic
por: Weber, Christopher M., et al.
Publicado: (2010)

Competitive Chemical Reaction Kinetic Model of Nucleosome Assembly Using the Histone Variant H2A.Z and H2A In Vitro
por: Zhao, Hongyu, et al.
Publicado: (2023)

BioSWR – Semantic Web Services Registry for Bioinformatics
por: Repchevsky, Dmitry, et al.
Publicado: (2014)

A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones
Publicado: (1987)

Expression of P. falciparum var Genes Involves Exchange of the Histone Variant H2A.Z at the Promoter
por: Petter, Michaela, et al.
Publicado: (2011)

Synthetic hyperacetylation of nucleosomal histones
por: Kajino, Hidetoshi, et al.
Publicado: (2020)

Nucleosome proteostasis and histone turnover
por: Arrieta, Adrian, et al.
Publicado: (2022)

Inter-nucleosomal communication between histone modifications for nucleosome phasing
por: Chen, Weizhong, et al.
Publicado: (2018)

Cancer-associated mutations of histones H2B, H3.1 and H2A.Z.1 affect the structure and stability of the nucleosome
por: Arimura, Yasuhiro, et al.
Publicado: (2018)

SWR/J mice are susceptible to alkylator-induced myeloid leukemia
por: Janke, M R, et al.
Publicado: (2013)

Maternal and developmental toxicity of Bisphenol-A in SWR/J mice
por: Mashay Al-Anazi, Khalid, et al.
Publicado: (2022)

SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites
por: Fukuto, Atsuhiko, et al.
Publicado: (2017)

INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers
por: Brahma, Sandipan, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_cqcbq1rm1eij7h28ic0mtq6eov