Brüser, Thomas and Deutzmann, Rainer and Dahl, Christiane (1998) Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli. FEMS MICROBIOLOGY LETTERS, 164 (2). pp. 329-336. ISSN 0378-1097, 1574-6968
Full text not available from this repository.Abstract
Proteins which are synthesized with a signal peptide containing a 'double-arginine' motif may be translocated across the bacterial cytoplasmic membrane by a mechanism that is different from the known Sec and signal recognition particle pathways. The function of the double-arginine motif as a determinant for this novel pathway was studied by expressions of gene constructs coding for the high potential iron-sulfur protein (HiPIP) from Chromatium vinosum D in Escherichia coli. When the protein was produced with its original double-arginine motif-containing signal peptide, it was in part translocated into the periplasm and thereby processed, as shown by immunoblots after cell fractionation and N-terminal sequencing of purified HiPIP. Processing was not inhibited significantly by 3 mM sodium azide, indicating that translocation of HiPIP occurs by a SecA-independent pathway. Translocation of HiPIP could je altered to the SecA-dependent mode when its signal peptide was substituted by that of PelB from Erwinia carotovora. When the HiPIP double-arginine motif (S (R) under bar (R) under bar DAVK) was introduced into the corresponding position of the PelB signal peptide, the transport pathway remained SecA-dependent. This indicates that additional determinants are required for translocation by the See-independent pathway. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | POTENTIAL IRON PROTEIN; CHROMATIUM-VINOSUM; SYNTHETIC GENE; SULFUR PROTEIN; EXPORT; SEQUENCE; MUTAGENESIS; HYDROGENASE; EXPRESSION; EXCHANGE; double-arginine motif signal peptide; protein translocation; iron-sulfur cluster; high potential iron-sulfur protein; Escherichia coli; Chromatium vinosum |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Rainer Deutzmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Feb 2023 10:33 |
| Last Modified: | 23 Feb 2023 10:33 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49669 |
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