Prokaryotic Utilization of the Twin-arginine Translocation Pathway: a Genomic Survey

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2003 Feb 4

PMID 12562823

Citations 106

Authors

Kieran Dilks

R Wesley Rose

Enno Hartmann

Mechthild Pohlschroder

Affiliations

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Abstract

The twin-arginine translocation (Tat) pathway, which has been identified in plant chloroplasts and prokaryotes, allows for the secretion of folded proteins. However, the extent to which this pathway is used among the prokaryotes is not known. By using a genomic approach, a comprehensive list of putative Tat substrates for 84 diverse prokaryotes was established. Strikingly, the results indicate that the Tat pathway is utilized to highly varying extents. Furthermore, while many prokaryotes use this pathway predominantly for the secretion of redox proteins, analyses of the predicted substrates suggest that certain bacteria and archaea secrete mainly nonredox proteins via the Tat pathway. While no correlation was observed between the number of Tat machinery components encoded by an organism and the number of predicted Tat substrates, it was noted that the composition of this machinery was specific to phylogenetic taxa.

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References

Bentley S, Chater K, Challis G, Thomson N, James K, Harris D . Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 2002; 417(6885):141-7. DOI: 10.1038/417141a. View

Ize B, Gerard F, Zhang M, Chanal A, Voulhoux R, Palmer T . In vivo dissection of the Tat translocation pathway in Escherichia coli. J Mol Biol. 2002; 317(3):327-35. DOI: 10.1006/jmbi.2002.5431. View

Ochsner U, Snyder A, Vasil A, Vasil M . Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc Natl Acad Sci U S A. 2002; 99(12):8312-7. PMC: 123064. DOI: 10.1073/pnas.082238299. View

DeLisa M, Samuelson P, Palmer T, Georgiou G . Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J Biol Chem. 2002; 277(33):29825-31. DOI: 10.1074/jbc.M201956200. View

Rose R, Bruser T, Kissinger J, Pohlschroder M . Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol Microbiol. 2002; 45(4):943-50. DOI: 10.1046/j.1365-2958.2002.03090.x. View

von Heijne G . The signal peptide. J Membr Biol. 1990; 115(3):195-201. DOI: 10.1007/BF01868635. View

Cline K, Ettinger W, Theg S . Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J Biol Chem. 1992; 267(4):2688-96. View

Niviere V, Wong S, Voordouw G . Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein. J Gen Microbiol. 1992; 138(10):2173-83. DOI: 10.1099/00221287-138-10-2173. View

Chaddock A, Mant A, Karnauchov I, Brink S, Herrmann R, Klosgen R . A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase. EMBO J. 1995; 14(12):2715-22. PMC: 398390. DOI: 10.1002/j.1460-2075.1995.tb07272.x. View

10.

Voelker R, Barkan A . Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 1995; 14(16):3905-14. PMC: 394469. DOI: 10.1002/j.1460-2075.1995.tb00062.x. View

11.

Berks B . A common export pathway for proteins binding complex redox cofactors?. Mol Microbiol. 1996; 22(3):393-404. DOI: 10.1046/j.1365-2958.1996.00114.x. View

12.

Nielsen H, Engelbrecht J, Brunak S, von Heijne G . Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997; 10(1):1-6. DOI: 10.1093/protein/10.1.1. View

13.

Altschul S, Madden T, Schaffer A, Zhang J, Zhang Z, Miller W . Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997; 25(17):3389-402. PMC: 146917. DOI: 10.1093/nar/25.17.3389. View

14.

Settles A, Yonetani A, Baron A, Bush D, Cline K, Martienssen R . Sec-independent protein translocation by the maize Hcf106 protein. Science. 1997; 278(5342):1467-70. DOI: 10.1126/science.278.5342.1467. View

15.

Pohlschroder M, Prinz W, Hartmann E, Beckwith J . Protein translocation in the three domains of life: variations on a theme. Cell. 1997; 91(5):563-6. DOI: 10.1016/s0092-8674(00)80443-2. View

16.

Santini C, Ize B, Chanal A, Muller M, Giordano G, Wu L . A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 1998; 17(1):101-12. PMC: 1170362. DOI: 10.1093/emboj/17.1.101. View

17.

Matlack K, Mothes W, Rapoport T . Protein translocation: tunnel vision. Cell. 1998; 92(3):381-90. DOI: 10.1016/s0092-8674(00)80930-7. View

18.

Weiner J, Bilous P, Shaw G, Lubitz S, Frost L, Thomas G . A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell. 1998; 93(1):93-101. DOI: 10.1016/s0092-8674(00)81149-6. View

19.

Sargent F, Bogsch E, Stanley N, Wexler M, Robinson C, Berks B . Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998; 17(13):3640-50. PMC: 1170700. DOI: 10.1093/emboj/17.13.3640. View

20.

Bogsch E, Sargent F, Stanley N, Berks B, Robinson C, Palmer T . An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem. 1998; 273(29):18003-6. DOI: 10.1074/jbc.273.29.18003. View