SOLUTION STRUCTURE AND INTERACTION ON THE CARBOXYL- TERMINAL DOMAIN OF ESCHERICHIA COLI RNA POLYMERASE $\alpha$ SUBUNIT STUDIED BY NMR

The three-dimensional structure of the carboxyl-terminal domain of the E.coli RNA polymerase $\alpha$ subunit, which is regarded as the contact site for transcription activator proteins and the promoter UP element, was determined by NMR spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. (omitted)