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The DsbA‐DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains
Author(s) -
Whitley Paul,
von Heijne Gunnar
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80481-9
Subject(s) - dsba , periplasmic space , protein disulfide isomerase , chemistry , disulfide bond , inner membrane , escherichia coli , biochemistry , biophysics , membrane protein , membrane , biology , gene
The DsbA and DsbB proteins of Escherichia coli are involved in facilitating the formation of disulfide bonds in periplasmic proteins. Here, we show that the rate of formation of a disulfide bond in the periplasmic domain of the inner membrane protein leader peptidase is reduced in dsbA and dsbB strains, whereas the rate of formation of a disulfide bond engineered into the membrane embedded domain of the same protein is completely unaffected by these mutations. We conclude that the Dsb proteins do not facilitate the formation of intramembraneous disulfides.