|
|
||||||||
Laboratory of Bacteriology, Rega Institute, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium
Correspondence
Jozef Anné
jozef.anne{at}rega.kuleuven.ac.be
Streptomyces are Gram-positive soil bacteria that are used industrially, not only as a source of medically important natural compounds, but also as a host for the secretory production of a number of heterologous proteins. A good understanding of the different secretion processes in this organism is therefore of major importance. The functionality of the recently discovered bacterial twin-arginine translocation (Tat) pathway has already been shown in Streptomyces lividans. Here, the aberrant phenotype of S. lividans
tatB and
tatC single mutants is described. Both mutants are characterized by a dispersed growth in liquid medium, an impaired morphological differentiation on solid medium and growth retardation. To reveal the extent to which the Tat pathway is used in Streptomyces, putative Tat-dependent precursor proteins of Streptomyces coelicolor, a very close relative of S. lividans, and of Streptomyces avermitilis, of which the genomes have been completely sequenced, were identified by a modified version of the TATFIND computer program designed by Rose and colleagues [Rose, R. W., Brüser, T., Kissinger, J. C. & Pohlschröder, M. (2002). Mol Microbiol 45, 943950]. A list of 230 precursor proteins was obtained; this is the highest number of putative Tat substrates found in any genome so far. In addition to the Streptomyces antibioticus tyrosinase, it was also demonstrated that the secretion of the S. lividans xylanase C is Tat-dependent. The predicted Tat substrates belong to a variety of protein classes, with a high number of proteins functioning in degradation of macromolecules, in binding and transport, and in secondary metabolism. Only a minor fraction of the proteins seem to bind a cofactor. The aberrant phenotype of the
tatB and
tatC mutants together with the high number of putative Tat-dependent substrates suggests that the Streptomyces Tat pathway has a distinct and more important role in protein secretion than in most other bacteria.
This article has been cited by other articles:
![]() |
C. Di Berardo, D. S. Capstick, M. J. Bibb, K. C. Findlay, M. J. Buttner, and M. A. Elliot Function and Redundancy of the Chaplin Cell Surface Proteins in Aerial Hypha Formation, Rodlet Assembly, and Viability in Streptomyces coelicolor J. Bacteriol., September 1, 2008; 190(17): 5879 - 5889. [Abstract] [Full Text] [PDF] |
||||
![]() |
I. Alexeev, A. Sultana, P. Mantsala, J. Niemi, and G. Schneider Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site PNAS, April 10, 2007; 104(15): 6170 - 6175. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. De Keersmaeker, K. Vrancken, L. Van Mellaert, J. Anne, and N. Geukens The Tat pathway in Streptomyces lividans: interaction of Tat subunits and their role in translocation Microbiology, April 1, 2007; 153(4): 1087 - 1094. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. A. Widdick, K. Dilks, G. Chandra, A. Bottrill, M. Naldrett, M. Pohlschroder, and T. Palmer The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor PNAS, November 21, 2006; 103(47): 17927 - 17932. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Geukens, S. Rao C. V., R. P. Mellado, F. Frederix, G. Reekmans, S. De Keersmaeker, K. Vrancken, K. Bonroy, L. Van Mellaert, E. Lammertyn, et al. Surface plasmon resonance-based interaction studies reveal competition of Streptomyces lividans type I signal peptidases for binding preproteins. Microbiology, May 1, 2006; 152(Pt 5): 1441 - 1450. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. E. Posey, T. M. Shinnick, and F. D. Quinn Characterization of the Twin-Arginine Translocase Secretion System of Mycobacterium smegmatis J. Bacteriol., February 15, 2006; 188(4): 1332 - 1340. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. McDonough, K. E. Hacker, A. R. Flores, M. S. Pavelka Jr, and M. Braunstein The Twin-Arginine Translocation Pathway of Mycobacterium smegmatis Is Functional and Required for the Export of Mycobacterial {beta}-Lactamases J. Bacteriol., November 15, 2005; 187(22): 7667 - 7679. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Li, P.-E. Jacques, M. G. Ghinet, R. Brzezinski, and R. Morosoli Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins Microbiology, July 1, 2005; 151(7): 2189 - 2198. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Blaudeck, P. Kreutzenbeck, M. Muller, G. A. Sprenger, and R. Freudl Isolation and Characterization of Bifunctional Escherichia coli TatA Mutant Proteins That Allow Efficient Tat-dependent Protein Translocation in the Absence of TatB J. Biol. Chem., February 4, 2005; 280(5): 3426 - 3432. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. O. d. O. Lucana, T. Schaa, and H. Schrempf The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB Microbiology, August 1, 2004; 150(8): 2575 - 2585. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |