Overlapping functions of components of a bacterial Sec-independent protein export pathway

The EMBO Journal
F SargentT Palmer

Abstract

We describe the identification of two Escherichia coli genes required for the export of cofactor-containing periplasmic proteins, synthesized with signal peptides containing a twin arginine motif. Both gene products are homologous to the maize HCF106 protein required for the translocation of a subset of lumenal proteins across the thylakoid membrane. Disruption of either gene affects the export of a range of such proteins, and a complete block is observed when both genes are inactivated. The Sec protein export pathway was unaffected, indicating the involvement of the gene products in a novel export system. The accumulation of active cofactor-containing proteins in the cytoplasm of the mutant strains suggests a role for the gene products in the translocation of folded proteins. One of the two HCF106 homologues is encoded by the first gene of a four cistron operon, tatABCD, and the second by an unlinked gene, tatE. A mutation previously assigned to the hcf106 homologue encoded at the tatABCD locus, mttA, lies instead in the tatB gene.

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Citations

Apr 4, 2008·Archives of Microbiology·Isabelle CaldelariFrank Sargent
Oct 8, 2009·Archives of Microbiology·Iris LükeFrank Sargent
Dec 2, 2005·Applied Microbiology and Biotechnology·Phatchaneeya ThammawongChatchai Tayapiwatana
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Jul 7, 2005·Extremophiles : Life Under Extreme Conditions·Kentaro Miyazaki
Aug 28, 2013·Extremophiles : Life Under Extreme Conditions·G SchmidM Thomm
Apr 2, 2005·Current Opinion in Microbiology·Ben C BerksFrank Sargent
Apr 2, 2013·Research in Microbiology·Roland Freudl
Apr 9, 2005·Trends in Microbiology·Tracy PalmerBen C Berks
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