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Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
Author(s) -
Jeruzalmi David,
Steitz Thomas A
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.14.4101
Subject(s) - polymerase , rna polymerase i , rna polymerase , t7 rna polymerase , rna dependent rna polymerase , microbiology and biotechnology , biology , rna polymerase iii , rna , rna polymerase ii , small nuclear rna , dna , genetics , gene , gene expression , bacteriophage , escherichia coli , promoter
The T7 RNA polymerase–T7 lysozyme complex regulates phage gene expression during infection of Escherichia coli . The 2.8 Å crystal structure of the complex reveals that lysozyme binds at a site remote from the polymerase active site, suggesting an indirect mechanism of inhibition. Comparison of the T7 RNA polymerase structure with that of the homologous pol I family of DNA polymerases reveals identities in the catalytic site but also differences specific to RNA polymerase function. The structure of T7 RNA polymerase presented here differs significantly from a previously published structure. Sequence similarities between phage RNA polymerases and those from mitochondria and chloroplasts, when interpreted in the context of our revised model of T7 RNA polymerase, suggest a conserved fold.