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Depletion of SecDF‐YajC causes a decrease in the level of SecG: implication for their functional interaction
Author(s) -
Kato Yoshihisa,
Nishiyama Ken-ichi,
Tokuda Hajime
Publication year - 2003
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/s0014-5793(03)00847-0
Subject(s) - chromosomal translocation , membrane , cysteine , in vitro , chemistry , in vivo , biophysics , microbiology and biotechnology , escherichia coli , biochemistry , biology , enzyme , genetics , gene
SecA and an apparatus comprising SecYEG and SecDF‐YajC complexes catalyze protein translocation across the Escherichia coli membrane. SecDF‐YajC and SecG facilitate membrane insertion of SecA, which is the driving force for protein translocation. Here we report that SecDF‐YajC depletion together with SecG depletion nearly completely inhibits protein translocation both in vivo and in vitro, although SecDF‐YajC had been thought to be unnecessary for in vitro translocation. The level of SecG in membranes decreased to about half upon SecDF‐YajC depletion and recovered to a normal level when SecDF‐YajC was expressed. SecDF‐YajC inhibited disulfide bond formation between two SecG molecules possessing a single cysteine residue. These results suggest functional interaction between SecDF‐YajC and SecG.