Journal article
Purified, Recombinant TagF Protein from Bacillus subtilis 168 Catalyzes the Polymerization of Glycerol Phosphate onto a Membrane Acceptor in Vitro *
Abstract
We report the first characterization of a recombinant protein involved in the polymerization of wall teichoic acid. Previously, a study of the teichoic acid polymerase activity associated with membranes from Bacillus subtilis 168 strains bearing thermosensitive mutations in tagB, tagD, and tagF implicated TagF as the poly(glycerol phosphate) polymerase (Pooley, H. M., Abellan, F. X., and Karamata, D. (1992) J. Bacteriol. 174, 646-649). In the …
Authors
Schertzer JW; Brown ED
Journal
Journal of Biological Chemistry, Vol. 278, No. 20, pp. 18002–18007
Publisher
Elsevier
Publication Date
5 2003
DOI
10.1074/jbc.m300706200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Bacillus subtilisCell MembraneDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliGenetic Complementation TestGlycerolGlycerophosphatesKineticsModels, ChemicalPeptidoglycanPlasmidsPolymersProtein BindingRecombinant ProteinsSubstrate SpecificityTeichoic AcidsTemperatureTime FactorsTransferases (Other Substituted Phosphate Groups)