We 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
- Introduction
- Talk outline
- Diverse structures of Fe/S clusters
- Coordination of Fe/S clusters
- Functions of Fe/S clusters: electron transfer
- Functions of Fe/S clusters: catalysis, regulation
- Functions of Fe/S clusters: S donor, stabilization
- How do we study Fe/S proteins in vitro?
- How do we study Fe/S proteins in vivo? (1)
- How do we study Fe/S proteins in vivo? (2)
- Active maturation of eukaryotic Fe/S proteins
- First model for cellular Fe/S protein biogenesis
- Biogenesis of cellular Fe/S proteins
- Biogenesis of mitochondrial Fe/S proteins I
- De novo Fe/S cluster assembly
- Structural glimpse: Human core Isc complex
- Biogenesis of mitochondrial Fe/S proteins II, III
- Mitochondrial Fe/S proteins biogenesis in yeast
- Mitochondrial Fe/S proteins biogenesis in man
- Multiple mitochondrial dysfunctions syndromes
- Conclusions and open questions
- Acknowledgments
Topics Covered
- Structure and functions of iron-sulfur (Fe/S) clusters and proteins
- Analysis of Fe/S proteins and their biogenesis
- Mechanisms of Fe/S protein assembly in mitochondria
- Mitochondrial “Fe/S diseases“
Links
Series:
Categories:
Talk Citation
Lill, R. (2018, March 29). Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 10, 2024, from https://doi.org/10.69645/OTWE7345.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Roland Lill has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria
Published on March 29, 2018
49 min
Other Talks in the Series: Mitochondria in Health and Disease
Transcript
Please wait while the transcript is being prepared...
0:00
Hello, my name is Roland Lill,
I'm a Professor of Cell Biology at
the Institute of Zytobiologie at the Philipps- Universitat of Marburg, in Germany.
In my lecture, I will try to give you an overview on what we learned over
the past two decades on the Biogenesis of Cellular Iron-Sulfur Proteins in Eukaryotes.
0:23
In part one of my lecture,
I will first provide you with a general overview on
the structure and function of Iron-Sulfur clusters and proteins in nature.
Then I will briefly introduce you into
the biochemical and spectroscopic methods of how
we can analyze Iron-Sulfur proteins and their biogenesis.
Next, I will concentrate on what we know about
the mechanisms of the Iron-Sulfur protein assembly in mitochondria.
This is then followed by a brief overview of
the so-called mitochondrial Iron-Sulfur diseases.
And finally, I will discuss a few open questions in this exciting research field.
In part two, I will cover the role of mitochondrion and assembly.
I will talk on cytosolic and nuclear Iron-Sulfur proteins,
the mechanisms of this process and about a number of
essential cellular processes intimately connected
to cytosolic and nuclear Iron-Sulfur protein biogenesis.
1:28
Iron-Sulfur clusters are among the oldest and most simple protein co-factors we know.
The simplest form of Iron-Sulfur clusters are
the rhombic 2Fe-2S clusters on the left,
and the cubic 4Fe-4S cluster on the right.
Together, they comprise more than 90% of the clusters we know, in the living world.
The clusters are usually coordinated by
the iron-ions to cysteine residues of the polypeptide chain.
However, we know other forms of Iron-Sulfur clusters such
as the 3Fe-4S or 4Fe-3S clusters,
where simply a 4Fe-4S cluster has lost either an iron or a sulfur-iron respectively,
for instance, in the latter case in oxygen resistant hydrogenase.
More complex Iron-Sulfur clusters are present for instance in the well
studied bacterial protein nitrogenase, which exists nitrogen.
Its P-cluster on the left is comprised of two 4Fe-4S clusters fused via a sulfur atom.
In the M or molybdenum cluster on the right,
one of the iron ions is replaced by another metal,
in this case molybdenum but can also be
vanadium giving rise to a rather complex cluster structure.
Hide