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Literature summary for 2.7.7.6 extracted from

  • King, R.A.; Markov, D.; Sen, R.; Severinov, K.; Weisberg, R.A.
    A conserved zinc binding domain in the largest subunit of DNA-dependent RNA polymerase modulates intrinsic transcription termination and antitermination but does not stabilize the elongation complex (2004), J. Mol. Biol., 342, 1143-1154.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C70A/C72H/C85A/C88H mutant enzyme is defective in intrinsic termination and antitermination in vitro. Mutation likely causes a recessive-lethal phenotype Escherichia coli
C70H mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype Escherichia coli
C72H mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype Escherichia coli
C85H mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype Escherichia coli
del70-88insGGGG mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype Escherichia coli
del74-84insGGGG mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc a conserved zinc binding domain in the largest subunit of DNA-dependent RNA polymerase modulates intrinsic transcription termination and antitermination but does not stabilize the elongation complex Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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