Registration for a live webinar on 'Precision medicine treatment for anticancer drug resistance' is now open.
See webinar detailsWe noted you are experiencing viewing problems
-
Check with your IT department that JWPlatform, JWPlayer and Amazon AWS & CloudFront are not being blocked by your network. The relevant domains are *.jwplatform.com, *.jwpsrv.com, *.jwpcdn.com, jwpltx.com, jwpsrv.a.ssl.fastly.net, *.amazonaws.com and *.cloudfront.net. The relevant ports are 80 and 443.
-
Check the following talk links to see which ones work correctly:
Auto Mode
HTTP Progressive Download Send us your results from the above test links at access@hstalks.com and we will contact you with further advice on troubleshooting your viewing problems. -
No luck yet? More tips for troubleshooting viewing issues
-
Contact HST Support access@hstalks.com
-
Please review our troubleshooting guide for tips and advice on resolving your viewing problems.
-
For additional help, please don't hesitate to contact HST support access@hstalks.com
We hope you have enjoyed this limited-length demo
This is a limited length demo talk; you may
login or
review methods of
obtaining more access.
Printable Handouts
Navigable Slide Index
- Intro slide
- The size of the human genome
- DNA compaction
- DNA packaging occurs at multiple levels
- The structure of the nucleosome
- 1984 to 1997
- Nucleosome architecture
- The nucleosome core particle
- Nucleosome structure, space filling
- Nucleosome structure, ribbon diagram
- Nucleosomes are symmetric
- Nucleosome architecture - the histone ooctamer
- The histones
- Histones are structurally and functionally bipartite
- The histone fold dimers bind DNA
- Each histone fold dimer organizes 30 bp of DNA
- H3-H4 and H2A-H2B are structurally conserved
- Histone fold extensions are structurally diverse
- Extensions and tails define nucleosome surface
- What holds the histone fold dimers together?
- H3 - H3 four-helix bundle
- H2B-H4 four-helix bundle
- The H2A docking domain
- H2A docking domain
- The H2A L1-L1 interface
- (H2A-H2B) forms two interfaces with (H3-H4)2
- Nucleosome assembly in vivo
- Nucleosome assembly - (H3-H4)2 tetramer
- Nucleosome assembly - (H3-H4)2 with DNA
- Nucleosome assembly - (H3-H4)2 and H2A-H2B(1)
- Nucleosome assembly - (H3-H4)2 and H2A-H2B(2)
- Nucleosome assembly- one additional dimer
- Nucleosome assembly - folded NCP
- The four core histones share the histone fold motif
- Histone tails are sites of reversible modifications
- Two histone tails emerge between two DNA gyres
- The H3 tail between two DNA gyres
- Multiple roles for the histone tails
- Formation of higher order structure
- H4 tail interactions with the acidic patch
- Protein-DNA interactions
- 14 attachment points at the minor groove of DNA
- Each histone dimer has three DNA binding sites
- Interactions at the protein-DNA interface (1)
- Interactions at the protein-DNA interface (2)
- Water molecules at the protein - DNA interface
- Water-mediated protein - DNA contacts
- Summary: Protein-DNA interaction
- Nucleosome architecture - DNA structure
- Non-uniform deformation of nucleosomal DNA
- Minor groove width fluctuations
- Minor groove width fluctuates with 10 bp periodicity
- The 'Slinky' Analogy
- Nucleosome architecture
- Beyond the nucleosome - uncharted territory
- The 30 nm fiber
- Models for the 30 nm fibers
- Chromatin higher order structure
- Chromatin structure is affected by many factors
- Chromatin-associated proteins
- Chromatin-associated proteins - unknown
- Summary
Topics Covered
- Chromatin and differential regulation of transcription
- Basic structure and properties of a nucleosome
- Current knowledge on higher order chromatin structures
Talk Citation
Luger, K. (2021, March 8). Introduction to chromatin structure [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 26, 2024, from https://doi.org/10.69645/KZVS2603.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Karolin Luger has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Update Available
The speaker addresses developments since the publication of the original talk. We recommend listening to the associated update as well as the lecture.
- Full lecture Duration: 41:30 min
- Update Interview Duration: 14:30 min
A selection of talks on Genetics & Epigenetics
Transcript
Please wait while the transcript is being prepared...
0:03
The eukaryotic genome is enormous,
not only in its information content,
but also in its sheer physical size.
The eukaryotic nucleus is only about five microns in diameter.
It has to contain a genome that,
if all pieced together,
would be about two meters in length.
As a simple analogy,
if the nucleus were the size of a golf ball,
it would contain about 10 miles of DNA.
0:26
As a consequence, each eukaryotic cell is faced with
a very daunting proposition of compacting its DNA to a massive degree.
The requirements are not only to package DNA into the nucleus,
but also to protect the genome while at the same time allowing
access to the information at the appropriate time by the cellular machinery.
DNA is found in complex with an equal mass of proteins to
form protein DNA complex collectively termed chromatin.
Histone proteins form the nucleosomes and
non-histone proteins are supposed to aid in further compaction.
1:11
DNA packaging in the eukaryotic cell occurs at multiple levels.
At the first organizational level,
DNA is wrapped around disk-shaped assembly of eight histones,
the so-called histone octamer,
to form the nucleosome.
Beads on a string-like structures of nucleosomes are
then further folded into nucleosome arrays,
or the so-called, 30-nanometre fiber.
This occurs via short-range inter-nucleosome interaction.
Linker histones then aid in the further compaction of
30-nanometer fibers to form higher-order structures and stably folded chromatin fibers.
Long-range fiber-fiber interactions are
responsible to form even higher condensed arrays of nucleosomes.
At the peak of the compaction,
the metaphase chromosome is found.