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Targeting signals for a bacterial Sec‐independent export system direct plant thylakoid import by the ΔpH pathway
Author(s) -
Wexler Margaret,
Bogsch Erik G.,
Klösgen Ralf Bernd,
Palmer Tracy,
Robinson Colin,
Berks Ben C.
Publication year - 1998
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(98)00790-x
Subject(s) - thylakoid , arginine , chloroplast , twin arginine translocation pathway , transport protein , bacteria , protein subunit , biochemistry , chemistry , biology , biophysics , microbiology and biotechnology , amino acid , genetics , gene
Preproteins targeted to the Sec‐independent protein transport systems of plant thylakoids and of bacteria both have unusual transfer peptides bearing a consensus twin‐arginine motif. Possible mechanistic similarity between the two Sec‐independent transport pathways was investigated by assessing the ability of bacterial twin‐arginine transfer peptides to direct thylakoid import. High efficiency import was observed. This process was demonstrated to occur specifically via the Sec‐independent ΔpH pathway and to depend on an intact twin‐arginine motif on the transfer peptide. These results provide strong evidence for the operation of mechanistically related Sec‐independent protein transport pathways in chloroplasts and bacteria.