REVIEW: Structural-Functional Analysis of Bacteriophage T7 RNA Polymerase

V. L. Tunitskaya and S. N. Kochetkov^*

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, 119991 Russia; fax: (095) 135-1405; E-mail: kochet@eimb.ru

^* To whom correspondence should be addressed.

Received April 18, 2002

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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 T7-transcription, and also the results of structural and functional studies by affinity modification and both random and site-directed mutagenesis techniques.

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KEY WORDS: bacteriophage T7, DNA-dependent RNA polymerase, structural-functional topography, affinity modification, mutagenesis

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