scholarly journals Type-II secretion pathway structural gene xpsE, xylanase- and cellulase secretion and virulence in Xanthomonas oryzae pv. oryzae

2005 ◽  
Vol 54 (1) ◽  
pp. 15-21 ◽  
Author(s):  
Q. H. Sun ◽  
J. Hu ◽  
G. X. Huang ◽  
C. Ge ◽  
R. X. Fang ◽  
...  
2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Helge M. Dietrich ◽  
Miriam Edel ◽  
Thea Bursac ◽  
Manfred Meier ◽  
Katrin Sturm-Richter ◽  
...  

AbstractThis study reveals that it is possible to secrete truncated versions of outer membrane cytochromes into the culture supernatant and that these proteins can provide a basis for the export of heterologously produced proteins. Different soluble and truncated versions of the outer membrane cytochrome MtrF were analyzed for their suitability to be secreted. A protein version with a very short truncation of the N-terminus to remove the recognition sequence for the addition of a lipid anchor is secreted efficiently to the culture supernatant, and moreover this protein could be further truncated by a deletion of 160 amino acid and still is detectable in the supernatant. By coupling a cellulase to this soluble outer membrane cytochrome, the export efficiency was measured by means of relative cellulase activity. We conclude that outer membrane cytochromes of S. oneidensis can be applied as transporters for the export of target proteins into the medium using the type II secretion pathway.


2000 ◽  
Vol 263 (6) ◽  
pp. 1031-1037 ◽  
Author(s):  
R. Riekki ◽  
T. Palomäki ◽  
O. Virtaharju ◽  
H. Kokko ◽  
M. Romantschuk ◽  
...  

2009 ◽  
Vol 75 (12) ◽  
pp. 4197-4201 ◽  
Author(s):  
Cristina Sánchez-Porro ◽  
Encarnación Mellado ◽  
Anthony P. Pugsley ◽  
Olivera Francetic ◽  
Antonio Ventosa

ABSTRACT The gene (cpo) encoding the extracellular protease CPI produced by the moderately halophilic bacterium Pseudoalteromonas ruthenica CP76 was cloned, and its nucleotide sequence was analyzed. The cpo gene encodes a 733-residue protein showing sequence similarity to metalloproteases of the M4 family. The type II secretion apparatus was shown to be responsible for secretion of the haloprotease CPI.


2006 ◽  
Vol 189 (1) ◽  
pp. 142-150 ◽  
Author(s):  
Ji Yang ◽  
Deborah L. Baldi ◽  
Marija Tauschek ◽  
Richard A. Strugnell ◽  
Roy M. Robins-Browne

ABSTRACT The gene cluster gspCDEFGHIJKLM codes for various structural components of the type II secretion pathway which is responsible for the secretion of heat-labile enterotoxin by enterotoxigenic Escherichia coli (ETEC). In this work, we used a variety of molecular approaches to elucidate the transcriptional organization of the ETEC type II secretion system and to unravel the mechanisms by which the expression of these genes is controlled. We showed that the gspCDEFGHIJKLM cluster and three other upstream genes, yghJ, pppA, and yghG, are cotranscribed and that a promoter located in the upstream region of yghJ plays a major role in the expression of this 14-gene transcriptional unit. Transcription of the yghJ promoter was repressed 168-fold upon a temperature downshift from 37°C to 22°C. This temperature-induced repression was mediated by the global regulatory proteins H-NS and StpA. Deletion mutagenesis showed that the promoter region encompassing positions −321 to +301 relative to the start site of transcription of yghJ was required for full repression. The yghJ promoter region is predicted to be highly curved and bound H-NS or StpA directly. The binding of H-NS or StpA blocked transcription initiation by inhibiting promoter open complex formation. Unraveling the mechanisms of regulation of type II secretion by ETEC enhances our understanding of the pathogenesis of ETEC and other pathogenic varieties of E. coli.


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