Modular organization of the catalytic center of RNA polymerase

AUTOR(ES)

Mustaev, Arkady

FONTE

The National Academy of Sciences of the USA

RESUMO

The Fe2+ ion that specifically replaces Mg2+ in the active center of RNA polymerase generates reactive hydroxyl radicals that cause highly localized cleavage of polypeptide chains. Mapping of the cleavage sites revealed the overall architecture of the active center. Nine distinct sites, five in the β subunit and four in the β′ subunit of Escherichia coli RNA polymerase, all at or near highly conserved sequence motifs, are brought together in the enzyme’s ternary structure within the distance of ≈1 nm from the active center Me2+. These sites are located in at least six different domains of the subunits, reflecting modular organization of the active center.

Documentos Relacionados

• Donation of catalytic residues to RNA polymerase active center by transcription factor Gre
• RNA polymerase of influenza virus. IV. Catalytic properties of the capped RNA endonuclease associated with the RNA polymerase.
• Modular organization of cellular networks
• Spatial organization of RNA polymerase II transcription in the nucleus
• Modular Organization of the Phd Repressor/Antitoxin Protein