Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria

Published on March 29, 2018   49 min

Other Talks in the Category: Metabolism & Nutrition

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.
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Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria

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