Back to Search
Start Over
Three Distinct Proteases Are Responsible for Overall Cell Surface Proteolysis in Streptococcus thermophilus.
- Source :
-
Applied & Environmental Microbiology . Dec2021, Vol. 87 Issue 23, p1-17. 17p. - Publication Year :
- 2021
-
Abstract
- The lactic acid bacterium Streptococcus thermophilus was believed to display only two distinct proteases at the cell surface, namely, the cell envelope protease PrtS and the housekeeping protease HtrA. Using peptidomics, we demonstrate here the existence of an additional active cell surface protease, which shares significant homology with the SepM protease of Streptococcus mutans. Although all three proteases--PrtS, HtrA, and SepM--are involved in the turnover of surface proteins, they demonstrate distinct substrate specificities. In particular, SepM cleaves proteins involved in cell wall metabolism and cell elongation, and its inactivation has consequences for cell morphology. When all three proteases are inactivated, the residual cell-surface proteolysis of S. thermophilus is approximately 5% of that of the wildtype strain. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00992240
- Volume :
- 87
- Issue :
- 23
- Database :
- Academic Search Index
- Journal :
- Applied & Environmental Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 153671883
- Full Text :
- https://doi.org/10.1128/AEM.01292-21