
GcvA interacts with both the α and σ subunits of RNA polymerase to activate the Escherichia coli gcvB gene and the gcvTHP operon
Author(s) -
Stauffer Lorraine T.,
Stauffer George V.
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2004.11.027
Subject(s) - operon , promoter , rna polymerase , sigma factor , microbiology and biotechnology , transcription factor ii d , rna polymerase ii , biology , specificity factor , transcription (linguistics) , gal operon , polymerase , rna polymerase i , rna polymerase ii holoenzyme , gene , rna , gene expression , escherichia coli , genetics , linguistics , philosophy
The glycine cleavage enzyme system in Escherichia coli provides one‐carbon units for cellular methylation reactions. The gcvB gene encodes two small RNAs that in turn regulate other genes. The GcvA protein is required for expression of both the gcvTHP (P gcvT ) and gcvB (P gcvB ) promoters. However, the architectures of the two promoters are different, with the P gcvT promoter representing a class III activator‐dependent promoter and the P gcvB promoter representing a class II activator‐dependent promoter. The RNA polymerase holoenzyme was examined for its role in transcription activation of the gcvTHP operon and the gcvB gene by the GcvA protein. The results suggest that GcvA interacts with the RNA polymerase α subunit for activation of the gcvTHP operon and interacts with the RNA polymerase σ subunit for activation of the gcvB gene.