The crystal structure of Thermus aquaticus RNA polymerase (RNAP) with 3.3 A
ngstrom resolution has recently been described. The high degree of sequence
similarity between T aquaticus RNAP and the prototypical RNAP from Escheri
chia coli invites comparison of the new structural data with genetic and bi
ochemical results that defined the interaction sites of E. coli RNAP with t
ranscription regulators.