scholarly journals INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Sandipan Brahma ◽  
Maheshi I. Udugama ◽  
Jongseong Kim ◽  
Arjan Hada ◽  
Saurabh K. Bhardwaj ◽  
...  
Keyword(s):  
Histone Dimers

scholarly journals Cross-linking of histones with dimethyl 3,3′-dithiobispropionimidate. Interference by a one-end reaction modifying histones at lysine amino groups

1984 ◽  
Vol 224 (3) ◽  
pp. 1019-1022
Author(s):  
E Kotthaus ◽  
W H Strätling
Keyword(s):  
Insoluble Fraction ◽  
Cross Linking ◽  
Amino Groups ◽  
Large Excess ◽  
Histone Dimers ◽  
Acid Solubility ◽  
Cross Linker ◽  
The Cross ◽  
Linker Molecules

We have studied the HClO4-solubility of histones H1 and H5 in hen erythrocyte nuclei after treatment with the cross-linker dimethyl 3,3′-dithiobispropionimidate (DTPI). The amount of acid-soluble, non-cross-linked, H1 and H5 histones was drastically decreased, and that of acid-soluble H1/H5 histone dimers went through an optimum as the DTPI concentration was raised. Incubation of the HClO4-insoluble fraction with 2-mercaptoethanol regenerated the acid-solubility of H1/H5 histones in this fraction. When purified H1/H5 histones were treated with increasing concentrations of DTPI under non-cross-linking conditions, the amount of HClO4-soluble histones also greatly decreased, but to a much lesser extent if the DTPI treatment was followed by reduction with 2-mercaptoethanol. This decrease was inversely correlated to the proportion of amino groups modified. It is concluded that, when the cross-linker was used in large excess, the cross-linking reaction competed with a one-end reaction modifying the histones at lysine amino groups by cross-linker molecules, of which the imidoester groups that had not reacted were hydrolysed. It is suggested that this modification produced the changes in acid-solubility.

Cofractionation of HMGB proteins with histone dimers

2014 ◽  
Vol 447 ◽  
pp. 98-106
Author(s):  
Qinqin Zhuang ◽  
Hugh Smallman ◽  
Stanley J. Lambert ◽  
Sirirath S. Sodngam ◽  
Colin D. Reynolds ◽  
...  
Keyword(s):  
Histone Dimers ◽  
Hmgb Proteins

scholarly journals Structure of a single-chain H2A/H2B dimer

2020 ◽  
Vol 76 (5) ◽  
pp. 194-198
Author(s):  
Christopher Warren ◽  
Jeffrey B. Bonanno ◽  
Steven C. Almo ◽  
David Shechter
Keyword(s):  
Chromatin Remodeling ◽  
Interacting Proteins ◽  
Structural Studies ◽  
Histone H2a ◽  
Nucleosome Assembly ◽  
Single Chain ◽  
Histone Octamer ◽  
C Terminus ◽  
Histone Dimers ◽  
Histone Modifying Enzymes

Chromatin is the complex assembly of nucleic acids and proteins that makes up the physiological form of the eukaryotic genome. The nucleosome is the fundamental repeating unit of chromatin, and is composed of ∼147 bp of DNA wrapped around a histone octamer formed by two copies of each core histone: H2A, H2B, H3 and H4. Prior to nucleosome assembly, and during histone eviction, histones are typically assembled into soluble H2A/H2B dimers and H3/H4 dimers and tetramers. A multitude of factors interact with soluble histone dimers and tetramers, including chaperones, importins, histone-modifying enzymes and chromatin-remodeling enzymes. It is still unclear how many of these proteins recognize soluble histones; therefore, there is a need for new structural tools to study non-nucleosomal histones. Here, a single-chain, tailless Xenopus H2A/H2B dimer was created by directly fusing the C-terminus of H2B to the N-terminus of H2A. It is shown that this construct (termed scH2BH2A) is readily expressed in bacteria and can be purified under non-denaturing conditions. A 1.31 Å resolution crystal structure of scH2BH2A shows that it adopts a conformation that is nearly identical to that of nucleosomal H2A/H2B. This new tool is likely to facilitate future structural studies of many H2A/H2B-interacting proteins.

scholarly journals Structure of a Single Chain H2A/H2B Dimer

2020 ◽  
Author(s):  
Christopher Warren ◽  
Jeffrey B. Bonanno ◽  
Steven C. Almo ◽  
David Shechter
Keyword(s):  
Chromatin Remodeling ◽  
Interacting Proteins ◽  
Structural Studies ◽  
Histone H2a ◽  
Nucleosome Assembly ◽  
Single Chain ◽  
Histone Octamer ◽  
C Terminus ◽  
Histone Dimers ◽  
Histone Modifying Enzymes

ABSTRACTChromatin is the complex assembly of nucleic acids and proteins that makes up the physiological form of the eukaryotic genome. The nucleosome is the fundamental repeating unit of chromatin, composed of ~147bp of DNA wrapped around a histone octamer formed by two copies of each core histone: H2A, H2B, H3 and H4. Prior to nucleosome assembly, and during histone eviction, histones are typically assembled into soluble H2A/H2B dimers and H3/H4 dimers and tetramers. A multitude of factors interact with soluble histone dimers and tetramers, including chaperones, importins, histone modifying enzymes, and chromatin remodeling enzymes. It is still unclear how many of these proteins recognize soluble histones; therefore, there is a need for new structural tools to study non-nucleosomal histones. Here we created a single-chain, tailless Xenopus H2A/H2B dimer by directly fusing the C-terminus of H2B to the N-terminus of H2A. We show that this construct (termed scH2BH2A) is readily expressed in bacteria and can be purified under non-denaturing conditions. A 1.31Å crystal structure of scH2BH2A shows that it adopts a conformation nearly identical to nucleosomal H2A/H2B. This new tool will facilitate future structural studies of a multitude of H2A/H2B-interacting proteins.

scholarly journals The ATP-Dependent Remodeler RSC Transfers Histone Dimers and Octamers through the Rapid Formation of an Unstable Encounter Intermediate

Biochemistry ◽  
2010 ◽  
Vol 49 (45) ◽  
pp. 9882-9890 ◽  
Author(s):  
Claire E. Rowe ◽  
Geeta J. Narlikar
Keyword(s):  
Histone Dimers ◽  
Rapid Formation

scholarly journals Histone dimers: a fundamental unit in histone assembly

1976 ◽  
Vol 3 (5) ◽  
pp. 1263-1276 ◽  
Author(s):  
R. Sperling ◽  
M. Bustin
Keyword(s):  
Fundamental Unit ◽  
Histone Dimers

scholarly journals Mechanical and structural properties of archaeal hypernucleosomes

2020 ◽  
Author(s):  
Bram Henneman ◽  
Thomas B Brouwer ◽  
Amanda M Erkelens ◽  
Gert-Jan Kuijntjes ◽  
Clara van Emmerik ◽  
...  
Keyword(s):  
Environmental Changes ◽  
Stacking Interactions ◽  
Dna Complexes ◽  
Left Handed ◽  
Histone Dimers ◽  
And Function ◽  
Dna Complex ◽  
Dna Substrate ◽  
Archaeal Histone

Abstract Many archaea express histones, which organize the genome and play a key role in gene regulation. The structure and function of archaeal histone–DNA complexes remain however largely unclear. Recent studies show formation of hypernucleosomes consisting of DNA wrapped around an ‘endless’ histone-protein core. However, if and how such a hypernucleosome structure assembles on a long DNA substrate and which interactions provide for its stability, remains unclear. Here, we describe micromanipulation studies of complexes of the histones HMfA and HMfB with DNA. Our experiments show hypernucleosome assembly which results from cooperative binding of histones to DNA, facilitated by weak stacking interactions between neighboring histone dimers. Furthermore, rotational force spectroscopy demonstrates that the HMfB–DNA complex has a left-handed chirality, but that torque can drive it in a right-handed conformation. The structure of the hypernucleosome thus depends on stacking interactions, torque, and force. In vivo, such modulation of the archaeal hypernucleosome structure may play an important role in transcription regulation in response to environmental changes.

scholarly journals ORC binds and remodels nucleosomes to specify MCM loading onto DNA

2021 ◽  
Author(s):  
Sai Li ◽  
Michael R. Wasserman ◽  
Olga Yurieva ◽  
Lu Bai ◽  
Michael E. O’Donnell ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Replication ◽  
Dna Sequence ◽  
Single Molecule ◽  
Origin Recognition Complex ◽  
Histone Dimers ◽  
Mcm Helicase ◽  
Eukaryotic Dna ◽  
Higher Eukaryotes ◽  
Origin Function

ABSTRACTSaccharomyces cerevisiae has been a faithful guide for study of eukaryotic DNA replication, as the numerous initiation and elongation proteins are conserved from yeast to human. However, there is a gap in our knowledge of why yeast uses a consensus DNA sequence at replication origins, while higher eukaryotes do not. The current study closes this gap. By direct single-molecule visualization, we show that the Origin Recognition Complex (ORC) searches for and stably binds nucleosomes, and that nucleosomes funtionalize ORC to load MCM helicase onto DNA, regardless of DNA sequence. Furthermore, we discover that ORC can remodel nucleosomes and expel H2A-H2B histone dimers, a heretofore unexpected function. Thus ORC helps create a chromatin environment permissive to origin function. The finding that ORC binding to nucleosomes leads to MCM loading at any DNA sequence is likely to generalize, and that higher eukaryotes follow this same paradigm for origin selection

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