TatAc, the third TatA subunit of Bacillus subtilis, can form active twin-arginine translocases with the TatCd and TatCy subunits

Applied and Environmental Microbiology

Volumn 78, Issue 14, 2012, Pages 4999-5001

  Monteferrante, Carmine G ^a   Baglieri, Jacopo ^b   Robinson, Colin ^b   van Dijl, Jan Maarten ^a  

^a UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PROTEINS; BACILLUS SUBTILIS; GRAM-POSITIVE BACTERIUM; PROTEIN SECRETION; TRANSLOCASES;

BIOTECHNOLOGY; MICROBIOLOGY;

ARGININE;

BACTERIAL PROTEIN; CARRIER PROTEIN;

BACTERIOLOGY; BACTERIUM; ENZYME ACTIVITY; PROTEIN; SECRETION; TRANSLOCATION;

ARTICLE; BACILLUS SUBTILIS; CHEMISTRY; ESCHERICHIA COLI; GENETICS; METABOLISM; PROTEIN SUBUNIT; PROTEIN TRANSPORT;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; ESCHERICHIA COLI; MEMBRANE TRANSPORT PROTEINS; PROTEIN SUBUNITS; PROTEIN TRANSPORT;

BACILLUS SUBTILIS; POSIBACTERIA;

EID: 84863731293     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01108-12     Document Type: Article

References (23)

1. Baglieri J, Beck D, Vasisht N, Smith CJ, Robinson C. 2012. Structure of the TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter. J. Biol. Chem. 287:7335-7344.
2. Barnett JP, et al. 2009. The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS J. 276:232-243.
3. Bernhardt TG, de Boer PA. 2003. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48:1171-1182.
4. Bogsch EG, et al. 1998. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273:18003-18006.
5. Bolhuis A, Mathers JE, Thomas JD, Barrett CML, Robinson C. 2001. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276:20213-20219.
6. Desvaux M, Hébraud M, Talon R, Henderson IR. 2009. Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol. 17:139-145.
7. Eijlander RT, Jongbloed JD, Kuipers OP. 2009. Relaxed specificity of the Bacillus subtilis TatAdCd translocase in Tat-dependent protein secretion. J. Bacteriol. 191:196-202.
8. Gohlke U, et al. 2005. The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc. Natl. Acad. Sci. U. S. A. 102:10482-10486.
9. Ize B, Stanley NR, Buchanan G, Palmer T. 2003. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol. Microbiol. 48:1183-1193.
10. Jongbloed JDH, van der Ploeg R, van Dijl JM. 2006. Bifunctional TatA subunits in minimal Tat protein translocases. Trends Microbiol. 14:2-4.
11. Jongbloed JDH, et al. 2004. Two minimal Tat translocases in Bacillus. Mol. Microbiol. 54:1319-1325.
12. Jongbloed JDH, et al. 2000. TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. J. Biol. Chem. 275: 41350-41357.
13. Jongbloed JDH, et al. 2002. Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis. J. Biol. Chem. 277:44068-44078.
14. Nicolas P, et al. 2012. Condition-dependent transcriptome reveals highlevel regulatory architecture in Bacillus subtilis. Science 335:1103-1106.
15. Pop O, Martin U, Abel C, Müller JP. 2002. The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system. J. Biol. Chem. 277:3268-3273.
16. Randall LL, Hardy SJ. 1986. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltosebinding protein in E. coli. Cell 46:921-928.
17. Robinson C, et al. 2011. Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochim. Biophys. Acta 1808:876-884.
18. Sargent F, et al. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:3640-3650.
19. Silvestro A, Pommier J, Pascal MC, Giordano G. 1989. The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers. Biochim. Biophys. Acta 999:208-216.
20. Tjalsma H, Bolhuis A, Jongbloed JD, Bron S, van Dijl JM. 2000. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64:515-547.
21. Tjalsma H, et al. 2004. Proteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome. Microbiol. Mol. Biol. Rev. 68: 207-233.
22. Warren G, Oates J, Robinson C, Dixon AM. 2009. Contributions of the transmembrane domain and a key acidic motif to assembly and function of the TatA complex. J. Mol. Biol. 388:122-132.
23. Yuan J, Zweers JC, van Dijl JM, Dalbey RE. 2010. Protein transport across and into cell membranes in bacteria and archaea. Cell. Mol. Life Sci. 67:179-199.