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A regulatory domain controls the transport activity of a twin‐arginine signal peptide
Author(s) -
Bowman Lisa,
Palmer Tracy,
Sargent Frank
Publication year - 2013
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/j.febslet.2013.09.005
Subject(s) - arginine , peptide , signal peptide , chemistry , signal (programming language) , domain (mathematical analysis) , microbiology and biotechnology , biophysics , biochemistry , peptide sequence , amino acid , biology , computer science , mathematics , gene , mathematical analysis , programming language
The twin‐arginine translocation (Tat) pathway is used by bacteria for the transmembrane transport of folded proteins. Proteins are targeted to the Tat translocase by signal peptides that have common tripartite structures consisting of polar n‐regions, hydrophobic h‐regions, and polar c‐regions. In this work, the signal peptide of [NiFe] hydrogenase‐1 from Escherichia coli has been studied. The hydrogenase‐1 signal peptide contains an extended n‐region that has a conserved primary structure. Genetic and biochemical approaches reveal that the signal peptide n‐region is essential for hydrogenase assembly and acts as a regulatory domain controlling transport activity of the signal peptide.