Molecular gymnastics: distortion of an RNA polymerase sigma factor.
A recent structure obtained by nuclear magnetic resonance (NMR) spectroscopy shows that the binding of a small phage factor to the sigma(70) subunit of Escherichia coli RNA polymerase induces an unprecedented remodeling of a region of sigma(70), converting a DNA-binding helix-turn-helix into a continuous pseudohelix. This conformational change suggests how the phage factor can function both as an inhibitor and co-activator of transcription.
Hinton
Deborah M
DM
Laboratory of Molecular and Cellular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, MD 20892-0830, USA. dhinton@helix.nih.gov
D017122:Bacteriophage T4 / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry* / Q000821:virology; D019077:Helix-Turn-Helix Motifs; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012808:Sigma Factor / Q000737:chemistry* / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
C078876:AsiA protein, Enterobacteria phage T4; D004268:DNA-Binding Proteins; C067996:MotA protein, Enterobacteria phage T4; D012808:Sigma Factor; D014157:Transcription Factors; D014764:Viral Proteins; C081775:RNA polymerase sigma 70; D012321:DNA-Directed RNA Polymerases