Structural characterisation of the tetrasome and histone chaperones
Lead Research Organisation:
University of Dundee
Department Name: College of Life Sciences
Abstract
DNA provides the genetic information that defines living organisms. However, at any one time only a proportion of genes are required to be active. An important step in regulating when genes are active is how accessible they are. In this proposal we will investigate the early steps in the packaging of DNA. This is fundamental to understanding how genes are regulated in humans and what goes wrong in a broad range of human diseases.
Technical Summary
The genomes of eukaryotes exisist as chromatin. The fundamental subunit of chromatin is the nuclesome. Nucleosomes are dissassembled and reassembled to allow access to genetic infromation for example during DNA replication. An early intermediate in the assembly of nucleosomes is the tetrasome, consisting of histones H3 and H4 associated with DNA. We aim to study the structure of the tetrasome using a range of techniques including SDSL, PELDOR and site directed crosslinking. Histone binding proteins known as histone chaperones are know to facilitate the assembly of tetrasomes. In order to gain insight as to how chaperones achieve this we will investigate how histones are bound by chaperones with the aim of gaining further insight into this important initial step in chromatin assembly.
Publications

Bowman A
(2014)
The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.
in Nucleic acids research

Bowman A
(2012)
Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4.
in Methods in molecular biology (Clifton, N.J.)

El Mkami H
(2014)
The spatial effect of protein deuteration on nitroxide spin-label relaxation: implications for EPR distance measurement.
in Journal of magnetic resonance (San Diego, Calif. : 1997)

Hammond CM
(2016)
The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.
in Nucleic acids research

Hammond CM
(2014)
Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH.
in Methods (San Diego, Calif.)

Narlikar GJ
(2013)
Mechanisms and functions of ATP-dependent chromatin-remodeling enzymes.
in Cell

Stevens MA
(2016)
The use of the Rx spin label in orientation measurement on proteins, by EPR.
in Physical chemistry chemical physics : PCCP

Zhang W
(2013)
Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1.
in Nature structural & molecular biology
Description | Structure and function of chromatin remodelling ATPase's and their dysfunction in in human disease. |
Amount | £1,232,837 (GBP) |
Funding ID | MR/S021647/1 |
Organisation | Medical Research Council (MRC) |
Sector | Public |
Country | United Kingdom |
Start | 03/2019 |
End | 03/2024 |
Title | Method for modelling using Distance constraints |
Description | Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model. |
Type Of Material | Model of mechanisms or symptoms - in vitro |
Year Produced | 2014 |
Provided To Others? | Yes |
Impact | The method has been published and so is available for other researchers to use. We have also used this approach to model the structure of a chaperone-histone complex. |
URL | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274318/ |
Title | Vps75 crystal structure |
Description | The co-ordinates of the histone chaperone Vps75 in a tetrameric conformation determined by X-ray diffraction |
Type Of Material | Database/Collection of data |
Provided To Others? | No |
Impact | This structure indicates that the Vps75 dimer can adopt different conformations which may affect its ability to interact with histones. The structure also indicates that Vps75 can adopt a tetrameric configuration. These findings provide a foundation understanding how Vps75 and likely nap1-fold proteins in general function to regulate chromatin assembly. This in turn influences gene expression which is fundamental to many biological processes. |
URL | http://www.rcsb.org/pdb/explore/explore.do?structureId=5AGC |
Description | Applying pulsed EPR to study chromatin dynamics |
Organisation | University of St Andrews |
Department | School of Physics and Astronomy |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | We have made material that has been used to make measurements using instruments located at St Andrews. |
Collaborator Contribution | The EPR group at St Andrews https://www.st-andrews.ac.uk/~mmwave/epr/ have made measurements on samples we have provided. |
Impact | https://www.ncbi.nlm.nih.gov/pubmed/19138067 https://www.ncbi.nlm.nih.gov/pubmed/19914933 https://www.ncbi.nlm.nih.gov/pubmed/20805036 https://www.ncbi.nlm.nih.gov/pubmed/21329878 https://www.ncbi.nlm.nih.gov/pubmed/23178455 https://www.ncbi.nlm.nih.gov/pubmed/25310878 https://www.ncbi.nlm.nih.gov/pubmed/27036862 https://www.ncbi.nlm.nih.gov/pubmed/28332978 https://www.ncbi.nlm.nih.gov/pubmed/30079888 The collaboration is interdisciplinary involving Physics and Molecular biology |
Start Year | 2009 |
Description | Inner Space Outer Space at the Mills Observatory |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | Local |
Primary Audience | Public/other audiences |
Results and Impact | The Mills Observatory in the heart of Dundee provides a unique location to develop, trial and offer public engagement activity that is immersive, uses multimodal-presentation techniques through a room-filling visual presentation screen, allowing visitors of all ages and abilities to engage with and explore the wonders of our micro and macro cosmos. This ambitious project is funded by the Centre for Gene Regulation and Expression at the University of Dundee by a Strategic Grant from the Wellcome Trust in partnership with Leisure and Culture Dundee and Dundee City Council. The project was initiated and is managed and run by the Dundee Imaging Facility the only multidisciplinary technology hub at the University which currently works with researchers from all of the STEMM subjects. It is being developed in collaboration with the School of Computing Computing's Augmentative and Alternative Communication (AAC) Research Group with input from Life Scientists, Physicists, Mathematicians and Astronomers from across the University. The new facilities allow accessible, interactive exploration of University research across all these disciplines. The technology used will also ensure that all audiences, especially people with impairments, can experience and interact with the presentations. |
Year(s) Of Engagement Activity | 2015,2016 |
URL | http://gre.dundee.ac.uk/outer-space-inner-space-mills-observatory/ |
Description | Open Doors day |
Form Of Engagement Activity | Participation in an open day or visit at my research institution |
Part Of Official Scheme? | Yes |
Geographic Reach | Local |
Primary Audience | Public/other audiences |
Results and Impact | Around 200 people attendend, members of the lab presented and interactive display describing protein puyrification, and participated in "coffeee with a scientist" session. Hopefully, interactions with members of public had some impact, but little evidence of this yet. Film crew attended gathering material for documentary describing research activity in Dundee |
Year(s) Of Engagement Activity | 2011,2012,2013,2014 |