Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.

@article{Tjalsma1998FunctionalAO,
  title={Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.},
  author={H. Tjalsma and A. Bolhuis and M. V. van Roosmalen and T. Wiegert and W. Schumann and C. Broekhuizen and W. Quax and G. Venem{\^a} and S. Bron and J. V. van Dijl},
  journal={Genes \& development},
  year={1998},
  volume={12 15},
  pages={
          2318-31
        }
}
Approximately 47% of the genes of the Gram-positive bacterium Bacillus subtilis belong to paralogous gene families. The present studies were aimed at the functional analysis of the sip gene family of B. subtilis, consisting of five chromosomal genes, denoted sipS, sipT, sipU, sipV, and sipW. All five sip genes specify type I signal peptidases (SPases), which are actively involved in the processing of secretory preproteins. Interestingly, strains lacking as many as four of these SPases could be… Expand
Detergent-independent in vitro activity of a truncated Bacillus signal peptidase.
SipY Is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 57 REFERENCES
Bacillus subtilis Contains Four Closely Related Type I Signal Peptidases with Overlapping Substrate Specificities
Type I signal peptidases of Bacillus subtilis
The Yeast SPC22/23 Homolog Spc3p Is Essential for Signal Peptidase Activity*
Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad.
  • M. T. Black
  • Biology, Medicine
  • Journal of bacteriology
  • 1993
The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
SEC11 is required for signal peptide processing and yeast cell growth
...
1
2
3
4
5
...