Back to Search
Start Over
Purification and Characterization of an Active N-Acetylglucosaminyltransferase Enzyme Complex from Streptococci.
- Source :
-
Applied & Environmental Microbiology . Dec2010, Vol. 76 Issue 24, p7966-7971. 6p. - Publication Year :
- 2010
-
Abstract
- A new family of bacterial serine-rich repeat glycoproteins can function as adhesins required for biofilm formation and pathogenesis in streptococci and staphylococci. Biogenesis of these proteins depends on a gene cluster coding for glycosyltransferases and accessory secretion proteins. Previous studies show that Fap1, a member of this family from Streptococcus parasanguinis, can be glycosylated by a protein glycosylation complex in a recombinant heterogeneous host. Here we report a tandem affinity purification (TAP) approach used to isolate and study protein complexes from native streptococci. This method demonstrated that a putative glycosyltransferase (Gtf2), which is essential for Fap1 glycosylation, readily copurified with another glycosyltransferase (Gtf1) from native S. parasanguinis. This result and the similar isolation of a homologous two-protein complex from Streptococcus pneumoniae indicate the biological relevance of the complexes to the glycosylation in streptococci. Furthermore, novel N-acetylglucosaminyltransferase activity was discovered for the complexes. Optimal activity required heterodimer formation and appears to represent a novel type of glycosylation. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00992240
- Volume :
- 76
- Issue :
- 24
- Database :
- Academic Search Index
- Journal :
- Applied & Environmental Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 57991494
- Full Text :
- https://doi.org/10.1128/AEM.01434-10