We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Sugar sulfates are not hydrolyzed by the acid-inducible sulfatase AslA from Salmonella enterica Enteritidis Nal<sup>R</sup> and Kentucky 3795 at pH 5.5.
- Authors
Ganguly, Arpeeta; Joerger, Rolf D.
- Abstract
The open reading frames SEN0085 and SeKA_A4361, from Salmonella enterica serovar Enteritidis NalR and serovar Kentucky 3795, respectively, corresponding to the acid-inducible sulfatase gene aslA from Salmonella enterica serovar Typhimurium, were previously suggested by microarray analysis to be differentially expressed under acid conditions. However, growth and enzyme activity tests in the present study demonstrated that both wild-type strains exhibited sulfatase activity with 4-nitrophenyl sulfate and 5-bromo-4-chloro-3 indolyl sulfate at pH 5.5. The acid sulfatase does not appear to be involved in sugar sulfate, tyrosine sulfate, 4-hydroxy-3-methoxyphenylglycol sulfate, heparin sulfate, or chondroitin sulfate hydrolysis at pH 5.5. Adhesion and invasion assays did not reveal differences between the serotypes and their corresponding aslA deletion mutants. Thus, the role and substrate(s) of AslA, a protein unique to salmonella and encoded in all sequenced Salmonella strains, remain elusive.
- Subjects
SALMONELLA enterica serovar enteritidis; ENZYME regulation; SALMONELLA enterica; NITROPHENYL compounds; SULFATES
- Publication
Canadian Journal of Microbiology, 2017, Vol 63, Issue 8, p739
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/cjm-2017-0059