This review summarizes our results of the structural and functional studies of bacteriophage T7 DNA-dependent RNA polymerase (T7 RNAP). Particular features of this enzyme (the single-subunit composition, relatively low molecular weight) make it the most convenient model for investigating the physicochemical aspects of transcription. The review discusses the main properties of T7 RNAP, interaction between the enzyme and promoter, principle stages of U-transcription, and also the results of structural and functional studies by affinity modification and both random and site-directed mutagenesis techniques.