title: Control of synthesis of wall teichoic acid in phosphate-starved cultures of Bacillus subtilis W23.
abstract: CDP-glycerol pyrophosphorylase, CDP-ribitol pyrophosphorylase and poly(ribitol phosphate) synthetase activities have been measured in cultures of Bacillus subtilis W23 as they became phosphate-starved either in batch culture or during changeover from potassium limitation to phosphate limitation in a chemostat. The results indicated that repression of synthesis of all three enzymes occurred at the onset of phosphate starvation and that this was accompanied by inhibition of inactivation of CDP-glycerol pyrophosphorylase and poly(ribitol phosphate) synthetase. These results show that the initial response to phosphate starvation involves more than inhibition of one enzyme as proposed by Glaser and Loewy [Glaser L. and Loewy, A. (1979) J. Biol. Chem. 254, 2184-2186]. Synthesis of both linkage unit and poly(ribitol phosphate) are inhibited independently.
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000378:metabolism; D010430:Pentosyltransferases / Q000378:metabolism; D010710:Phosphates / Q000494:pharmacology; D013682:Teichoic Acids / Q000096:biosynthesis* / Q000378:metabolism; D017855:Transferases (Other Substituted Phosphate Groups)
chemical_list: D009702:Nucleoside Diphosphate Sugars; D010710:Phosphates; D013682:Teichoic Acids; D010430:Pentosyltransferases; D009713:Nucleotidyltransferases; C020675:glycerol-3-phosphate cytidylyltransferase; C032634:D-ribitol-5-phosphate cytidylyltransferase; D017855:Transferases (Other Substituted Phosphate Groups); C022719:CDPribitol ribitolphosphotransferase