Applications of catalyzed cytoplasmic disulfide bond formation
|Author:||Saaranen, Mirva J.1; Ruddock, Lloyd W.1|
1Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Aapistie 7, 90220 Oulu, Finland
|Online Access:||PDF Full Text (PDF, 7.5 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe202103046550
|Publish Date:|| 2021-03-04
Disulfide bond formation is an essential post-translational modification required for many proteins to attain their native, functional structure. The formation of disulfide bonds, otherwise known as oxidative protein folding, occurs in the endoplasmic reticulum and mitochondrial inter-membrane space in eukaryotes and the periplasm of prokaryotes. While there are differences in the molecular mechanisms of oxidative folding in different compartments, it can essentially be broken down into two steps, disulfide formation and disulfide isomerization. For both steps, catalysts exist in all compartments where native disulfide bond formation occurs. Due to the importance of disulfide bonds for a plethora of proteins, considerable effort has been made to generate cell factories which can make them more efficiently and cheaper. Recently synthetic biology has been used to transfer catalysts of native disulfide bond formation into the cytoplasm of prokaryotes such as Escherichia coli. While these engineered systems cannot yet rival natural systems in the range and complexity of disulfide-bonded proteins that can be made, a growing range of proteins have been made successfully and yields of homogenously folded eukaryotic proteins exceeding g/l yields have been obtained. This review will briefly give an overview of such systems, the uses reported to date and areas of future potential development, including combining with engineered systems for cytoplasmic glycosylation.
Biochemical Society transactions
|Pages:||1223 - 1231|
|Type of Publication:||
A2 Review article in a scientific journal
|Field of Science:||
1182 Biochemistry, cell and molecular biology
© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society. This is an Accepted Manuscript of an article published in Biochemical Society Transactions. The final authenticated version is available online at: https://doi.org/10.1042/BST20190088.