4.6 Article

Mechanism of curaxin-dependent nucleosome unfolding by FACT

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

The fork protection complex recruits FACT to reorganize nucleosomes during replication

Barbara Safaric et al.

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 Biology

Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT

Anastasiia L. Sivkina et al.

Summary: Sivkina et al. characterized the interaction between S. cerevisiae histone chaperone FACT and the nucleosome core particle. They found that FACT adopts a more open geometry in the presence of Nhp6, and together they unfold nucleosomes. Nhp6 alters the structure of FACT and the properties of nucleosomes to support nucleosome unfolding.

COMMUNICATIONS BIOLOGY (2022)

Review Biochemistry & Molecular Biology

Transcription by RNA polymerase II and the CTD-chromatin crosstalk

Neha Singh et al.

Summary: The epigenetic phenomenon plays a role in the phenotypic variation of organisms by regulating the transcription of protein coding genes. The carboxy terminal domain (CTD) of RNA Polymerase II is thought to bind different protein complexes involved in mRNA biogenesis and export. The epigenetic modifications of CTD mediate its interaction with chromatin and influence histone modifications.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2022)

Article Cell Biology

H3-H4 histone chaperones and cancer

Dominique Ray-Gallet et al.

Summary: Histone chaperones play a crucial role in regulating chromatin structure and function. Dysregulation of these chaperones in cancer can affect tumor initiation and progression. Recent studies have focused on H3-H4 histone chaperones and their roles in various cancers, indicating their potential as tumor-promoting factors and useful biomarkers for clinical applications. The imperfect compensation between H3-H4 histone chaperones favors tumor progression through the stimulation of the Epithelial mesenchymal transition (EMT) or the Alternative lengthening of telomeres (ALT) pathway. Initial studies have also identified therapies targeting H3-H4 histone chaperones for cancer treatment.

CURRENT OPINION IN GENETICS & DEVELOPMENT (2022)

Article Multidisciplinary Sciences

ADAR1 masks the cancer immunotherapeutic promise of ZBP1-driven necroptosis

Ting Zhang et al.

Summary: ADAR1 is a determinant of resistance to ICB therapy by repressing immunogenic dsRNA and Z-RNA. CBL0137 is a small molecule that activates ZBP1, reverses ICB unresponsiveness, and induced necroptosis.

NATURE (2022)

Article Biochemistry & Molecular Biology

Structural basis of nucleosome transcription mediated by Chd1 and FACT

Lucas Farnung et al.

Summary: Structural and functional analyses of RNA polymerase II-nucleosome complexes reveal the mechanisms by which Chd1 and FACT facilitate Pol II transcription through nucleosomes with the presence of elongation factors Spt4/5 and TFIIS. Cryo-EM structures show Pol II transcription exposing histones bound by Spt5, releasing inhibitory DNA-binding region of Chd1, and generating unraveled nucleosomes binding FACT. These results suggest Pol II progression through nucleosomes activates Chd1, enables FACT binding, and triggers transfer of FACT and histones to upstream DNA.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2021)

Article Multidisciplinary Sciences

FACT caught in the act of manipulating the nucleosome

Yang Liu et al.

NATURE (2020)

Article Biochemistry & Molecular Biology

The role of FACT in managing chromatin: disruption, assembly, or repair?

Tim Formosa et al.

NUCLEIC ACIDS RESEARCH (2020)

Article Biochemistry & Molecular Biology

Histone chaperone FACT FAcilitates Chromatin Transcription: mechanistic and structural insights

Keda Zhou et al.

CURRENT OPINION IN STRUCTURAL BIOLOGY (2020)

Article Microscopy

MicroED data collection with SerialEM

M. Jason de la Cruz et al.

ULTRAMICROSCOPY (2019)

Article Biochemical Research Methods

Software tools for automated transmission electron microscopy

Martin Schorb et al.

NATURE METHODS (2019)

Article Multidisciplinary Sciences

Structural visualization of key steps in nucleosome reorganization by human FACT

Kouta Mayanagi et al.

SCIENTIFIC REPORTS (2019)

Review Biochemistry & Molecular Biology

Structure and function of the histone chaperone FACT - Resolving FACTual issues

Katerina Gurova et al.

BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS (2018)

Article Multidisciplinary Sciences

Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins

Han-Wen Chang et al.

SCIENCE ADVANCES (2018)

Review Cell Biology

Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes

Cedric R. Clapier et al.

NATURE REVIEWS MOLECULAR CELL BIOLOGY (2017)

Article Biochemistry & Molecular Biology

FACT is a sensor of DNA torsional stress in eukaryotic cells

Alfiya Safina et al.

NUCLEIC ACIDS RESEARCH (2017)

Article Biochemistry & Molecular Biology

Large-scale ATP-independent nucleosome unfolding by a histone chaperone

Maria E. Valieva et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)

Article Biochemistry & Molecular Biology

Large-scale ATP-independent nucleosome unfolding by a histone chaperone

Maria E. Valieva et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)

Article Biochemical Research Methods

Structure of the human histone chaperone FACT Spt16 N-terminal domain

G. Marciano et al.

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS (2016)

Review Biochemistry & Molecular Biology

Mechanism of transcription through a nucleosome by RNA polymerase II

Olga I. Kulaeva et al.

BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS (2013)

Article Multidisciplinary Sciences

Histone chaperone FACT action during transcription through chromatin by RNA polymerase II

Fu-Kai Hsieh et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)

Article Cell Biology

Curaxins: Anticancer Compounds that Simultaneously Suppress NF-κB and Activate p53 by Targeting FACT

Alexander V. Gasparian et al.

SCIENCE TRANSLATIONAL MEDICINE (2011)

Article Biochemistry & Molecular Biology

Crystal Structures of Nucleosome Core Particles Containing the '601' Strong Positioning Sequence

Dileep Vasudevan et al.

JOURNAL OF MOLECULAR BIOLOGY (2010)

Article Biochemical Research Methods

PLATINUM: a web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes

Timothy V. Pyrkov et al.

BIOINFORMATICS (2009)

Article Biochemistry & Molecular Biology

yFACT Induces Global Accessibility of Nucleosomal DNA without H2A-H2B Displacement

Hua Xin et al.

MOLECULAR CELL (2009)

Article Biochemistry & Molecular Biology

Mechanism of chromatin remodeling and recovery during passage of RNA polymerase II

Olga I. Kulaeva et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2009)

Article Multidisciplinary Sciences

The FACT Spt16 peptidase domain is a histone H3-H4 binding module

Tobias Stuwe et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)

Article Biochemistry & Molecular Biology

PIC: Protein Interactions Calculator

K. G. Tina et al.

NUCLEIC ACIDS RESEARCH (2007)

Article Biochemistry & Molecular Biology

EMAN2: An extensible image processing suite for electron microscopy

Guang Tang et al.

JOURNAL OF STRUCTURAL BIOLOGY (2007)

Article Chemistry, Multidisciplinary

UCSF chimera - A visualization system for exploratory research and analysis

EF Pettersen et al.

JOURNAL OF COMPUTATIONAL CHEMISTRY (2004)

Article Multidisciplinary Sciences

FACT facilitates transcription-dependent nucleosome alteration

R Belotserkovskaya et al.

SCIENCE (2003)

Article Chemistry, Multidisciplinary

HADDOCK: A protein-protein docking approach based on biochemical or biophysical information

C Dominguez et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)