L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase

MARIA CECILIA MANSILLA; DE MENDOZA, D.

JOURNAL OF BACTERIOLOGY

American Society for Microbiology

Lugar: Washington, DC; Año: 1997 vol. 179 p. 976 - 981

0021-9193

Random Tn917 mutagenesis of Bacillus subtilis followed by selection of lipoic acid auxotrophs led to theisolation of the cysH gene. The gene was sequenced and found to encode a phosphoadenylylsulfate sulfotransferasewith a molecular mass of 27 kDa. Expression of lacZ fused to the cysH promoter was repressed bycysteine and sulfide and induced by sulfur limitation, indicating that cysH is controlled at the level oftranscription.