An Engineered Pathway for the Formation of Protein Disulfide Bonds-Reference-Cited by-同舟云学术

An Engineered Pathway for the Formation of Protein Disulfide Bonds

Published:2004-02-20 Issue:5661 Volume:303 Page:1185-1189
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Masip Lluis¹²³⁴⁵,Pan Jonathan L.¹²³⁴⁵,Haldar Suranjana¹²³⁴⁵,Penner-Hahn James E.¹²³⁴⁵,DeLisa Matthew P.¹²³⁴⁵,Georgiou George¹²³⁴⁵,Bardwell James C. A.¹²³⁴⁵,Collet Jean-François¹²³⁴⁵

Affiliation:

1. Department of Chemical Engineering and Institute for Cell and Molecular Biology, University of Texas, Austin, TX 78712, USA.

2. Department of Biomedical Engineering, University of Texas, Austin, TX 78712, USA.

3. Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

4. Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI 48109, USA.

5. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Abstract

We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is a monomeric disulfide reductase, into a [2Fe-2S] bridged dimer capable of catalyzing O 2 -dependent sulfhydryl oxidation in vitro. Expression of the mutant protein in Escherichia coli with oxidizing cytoplasm and secretion via the Tat pathway restored disulfide bond formation in strains that lacked the complete periplasmic oxidative machinery (DsbA and DsbB). The evolution of [2Fe-2S] thioredoxin illustrates how mutations within an existing scaffold can add a cofactor and markedly change protein function.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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