Evolution and Diversity of Pathways for Disulfide Bond Formation and Reduction

 


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Air date: Wednesday, December 03, 2008, 3:00:00 PM
Category: Wednesday Afternoon Lectures
Description: We have evolved E. coli such that it can survive the absence of its essential glutathione and thioredoxin pathways ordinarily required for reduction of cytoplasmic disulfide bonds. These studies reveal remarkable flexibility of certain enzymes in the bacteria and lead to the discovery of similarly evolved enzymes already present in other bacteria. Structural disulfide bonds in proteins are found in many bacteria in extracellular compartments such as the periplasm.

Using a bioinformatic approach, we have proposed that there is significant diversity in the ability of bacteria to make structural disulfide bonds in proteins and in the machinery they use to make them. In particular, a large number of bacteria utilize a homologue of human vitamin K epoxide reductase (VKOR) to oxidize their DsbA in contrast to many others, such as E. coli, which use the protein DsbB. Bacterial VKOR shows remarkable similarities in properties to its human homologue, which is involved in blood clotting and is the target of Warfarin.

The NIH Director's Wednesday Afternoon Lecture Series includes weekly scientific talks by some of the top researchers in the biomedical sciences worldwide.
Author: Jonathan R. Beckwith
Runtime: 60 minutes
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CIT File ID: 14808
CIT Live ID: 7023
Permanent link: http://videocast.nih.gov/launch.asp?14808

 

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