Structural analysis of the yeast SWI/SNF chromatin remodeling complex

  title={Structural analysis of the yeast SWI/SNF chromatin remodeling complex},
  author={Corey L. Smith and Rachel A. Horowitz-Scherer and Joan Frances Flanagan and Christopher L. F. Woodcock and Craig L. Peterson},
  journal={Nature Structural Biology},
Elucidating the mechanism of ATP-dependent chromatin remodeling is one of the largest challenges in the field of gene regulation. One of the missing pieces in understanding this process is detailed structural information on the enzymes that catalyze the remodeling reactions. Here we use a combination of subunit radio-iodination and scanning transmission electron microscopy to determine the subunit stoichiometry and native molecular weight of the yeast SWI/SNF complex. We also report a three… 
Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription.
Electron microscopy studies of nucleosome remodelers.
Multiple functions of SWI/SNF chromatin remodeling complex in plant-pathogen interactions
Multiple functions of the SWI/SNF complex in eukaryotes are discussed in regulating gene transcription, mRNA splicing, and DNA damage response and the potentials in exploiting chromatin remodeling for management of crop disease are presented.
SWI/SNF Chromatin-remodeling Factors: Multiscale Analyses and Diverse Functions*
The role of SWI/SNF in human diseases, including cancer and viral infections is addressed; recent genomic and proteomic advances are highlighted; and the biochemistry of these complex enzymes is reviewed.
Mechanism(s) of SWI/SNF‐Induced Nucleosome Mobilization
Impediments to DNA access due to assembly of the eukaryotic genome into chromatin are in part overcome by the activity of ATP‐dependent chromatin‐remodeling complexes. These complexes employ energy
Structural analyses of the chromatin remodeling enzymes INO80-C and SWR-C
EM studies define the position of the Arp8/Arp4/Act1 module within INO80-C, and it is found that this module enhances nucleosome binding affinity but is largely dispensable for remodeling activities.
Studies on the mechanism of nucleosome remodeling by RSC and SWI/SNF
It is demonstrated that the docking domain of histone H2A is essential for SWI/SNF and RSC induced nucleosome sliding and the reason for inability of these nucleosomes to slide is due to a faulty generation of ‘Remosome' intermediates.
Structural biochemistry of the INO80 chromatin remodeler reveals an unexpected function of its two subunits Arp4 and Arp8
The goal of this study was to elucidate the functional architecture of the INO80 complex by using a hybrid methods approach and it is shown that Arp4 is able to inhibit actin polymerization and to depolymerize actin filaments most likely by complex formation with monomeric ADP-actin via the barbed end.


The SWI-SNF complex: a chromatin remodeling machine?
Structural analysis of the RSC chromatin-remodeling complex
Electron microscopy of the RSC chromatin-remodeling complex reveals a ring of protein densities around a central cavity that could explain the ability of RSC to expose nucleosomal DNA in the presence of ATP without loss of associated histones.
Direct Imaging of Human SWI/SNF-Remodeled Mono- and Polynucleosomes by Atomic Force Microscopy Employing Carbon Nanotube Tips
Both the repositioning and structural alteration of nucleosomes are important aspects of hSWI/SNF action on polynucleosomes, and ultrahigh-resolution carbon nanotube tip atomic force microscopy was used to examine the products of remodeling reactions carried out by the human SWI/ SNF complex.
ATP-Dependent Chromatin-Remodeling Complexes
An organized listing of the ATP-dependent chromatin-remodeling complexes described to date and the relationships between their subunits is provided and the relationship between these complexes and the HAT complexes is examined.
Nucleosome disruption and enhancement of activator binding by a human SW1/SNF complex
It is shown that a partially purified hSWI/SNF complex mediates the ATP-dependent disruption of a nucleosome, thereby enabling the activators, GAL 4–VP16 and GAL4–AH, to bind within aucleosome core.
Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex.
It is shown that the purified SWI/SNF complex is composed of 10 subunits and includes the SWI1, SWI2/ SNF2, SWi3, SNF5, and SNF6 gene products, and suggests that a primary role of the SWi/SNf complex is to promote activator binding to nucleosomal DNA.
The SWI/SNF Complex Creates Loop Domains in DNA and Polynucleosome Arrays and Can Disrupt DNA-Histone Contacts within These Domains
The data indicate that the action of one SWI/SNF complex on an array of nucleosomes can lead to the formation of a region where multipleucleosomes are disrupted, and nucleosome disruption by SWI-SNF results in a loss of DNA content from the nucleosomal DNA.
Crystal structure of the nucleosome core particle at 2.8 Å resolution
The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a
DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase.
  • D. Kelleher, R. Gilmore
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
The demonstration that D AD1 is a subunit of the OST suggests that induction of a cell death pathway upon loss of DAD1 in the tsBN7 cell line reflects the essential nature of N-linked glycosylation in eukaryotes.