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Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA
Author(s) -
Houben Edith N.G.,
Scotti Pier A.,
Valent Quido A.,
Brunner Josef,
de Gier Jan-Willem L.,
Oudega Bauke,
Luirink Joen
Publication year - 2000
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(00)01735-x
Subject(s) - signal recognition particle , escherichia coli , translocase , inner membrane , membrane , transmembrane domain , membrane protein , transmembrane protein , vesicle , biophysics , chemistry , biology , microbiology and biotechnology , signal peptide , biochemistry , recombinant dna , chromosomal translocation , gene , receptor
Targeting and assembly of the Escherichia coli inner membrane protein leader peptidase (Lep) was studied using a homologous in vitro targeting/translocation assay. Assembly of full‐length Lep was efficient in the co‐translational presence of membrane vesicles and hardly occurred when membranes were added post‐translationally. This is consistent with the signal recognition particle‐dependent targeting of Lep. Crosslinking experiments showed that the hydrophilic region P1 of nascent membrane‐inserted Lep 100‐mer was in the vicinity of SecA and SecY, whereas the first transmembrane domain H1 was in the vicinity of YidC. These results suggested that YidC, together with the Sec translocase, functions in the assembly of Lep. YidC might be a more generic component in the assembly of inner membrane proteins.