NIH VideoCast - Evolution and Diversity of Pathways for Disulfide Bond Formation and Reduction

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Evolution and Diversity of Pathways for Disulfide Bond Formation and Reduction

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Air date:	Wednesday, December 3, 2008, 3:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 113 * This only includes stats from October 2011 and forward.
Category:	WALS - Wednesday Afternoon Lectures
Runtime:	01:11:42
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
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.

NLM Title:	Evolution and diversity of pathways for disulfide bond formation and reduction / Jonathan R. Beckwith.
Author:	Beckwith, Jonathan R. National Institutes of Health (U.S.)
Publisher:
Abstract:	(CIT): 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.
Subjects:	Disulfides--metabolism Escherichia coli Proteins--metabolism
Publication Types:	Lecture Webcast
NLM Classification:	QV 280
NLM ID:	101493074
CIT Live ID:	7023
Permanent link:	https://videocast.nih.gov/watch=7023

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