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Characterization of the ams I gene product as a low molecular weight acid phosphatase controlling exopolysaccharide synthesis of Erwinia amylovora
Author(s) -
Bugert Peter,
Geider Klaus
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01398-1
Subject(s) - biochemistry , erwinia , gene product , phosphatase , biology , gene , activator (genetics) , acid phosphatase , escherichia coli , microbiology and biotechnology , gene expression , enzyme , chemistry
The ams region, responsible for amylovoran synthesis of the fireblight pathogen Erwinia amylovora , contains the gene ams I encoding a 144 amino acid protein with homology to mammalian low molecular weight acid phosphatases [Bugert and Geider (1995) Mol. Microbiol. 15, 917–933]. A DNA fragment with ams I was cloned under the control of the lac promoter on a high copy number plasmid. The gene product of ams I is about 17 kDa in a protein expression system and had the enzymatic activity of an acid phosphatase. This is the first report about a low molecular weight acid phosphatase activity in prokaryotes. As part of the large ams transcript, expression of ams I was affected by the activator proteins RcsA and RcsB. Overexpression of ams I in E. amylovora caused a strong increase of acid phosphatase activity, but additionally a strong reduction in EPS synthesis, phenotypically similar to a mutation in the gene. The gene product may participate in changes of phosphorylation required for the biosynthesis of EPS such as recycling the lipid carrier diphosphate to the monophosphate form.