Article Abstract:
Crystal structure analysis of the RNA polymerase II and the transcription elongation factor TFIIS complex reveals that TFIIS extends to the polymerase active site and two acidic amino acid residues in a TFIIS loop complement the RNA polymerase active site enabling it to cleave mRNA by positioning metal ion and water molecule. Data also indicate that TFIIS induces extensive structural changes in the enzyme.
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Article Abstract:
The crystal structures of the apo-initiator binding domain and initiator binding domain-initiator complexes and the c-terminal domain of the initiator binding protein 39 show winged-helix motif and a scaffold similar to ETS-family proteins for initiator binding domains. Data point out that binding of initiator binding protein 39 to the initiator recruits RNA polymerase II and initiates transcription.
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Article Abstract:
Crystal structure analysis of the Escherichia coli core RNA polymerase bound to the transcription elongation factor GreB indicates that the GreB N-terminal coiled-coil domian extends to the enzyme active site. Data suggest that conserved acidic amino acid residues at the tip of the Gre factor modify RNA polymerse active site leading to catalysis of cleavage activity by the enzyme.
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