title: Modulation of RNA polymerase activity through the trigger loop folding.
abstract: Folding of the trigger loop of RNA polymerase promotes nucleotide addition through creating a closed, catalytically competent conformation of the active center. Here, we discuss the impact of adjacent RNA polymerase elements, including the F loop and the jaw domain, as well as external regulatory factors on the trigger loop folding and catalysis.
authors.affiliation: Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, Russia.
authors.forename: Nataliya
authors.initials: N
authors.lastname: Miropolskaya
authors.forename: Vadim
authors.initials: V
authors.lastname: Nikiforov
authors.forename: Saulius
authors.initials: S
authors.lastname: Klimasauskas
authors.forename: Irina
authors.initials: I
authors.lastname: Artsimovitch
authors.forename: Andrey
authors.initials: A
authors.lastname: Kulbachinskiy
mesh_terms: D000595:Amino Acid Sequence; D055162:Biocatalysis; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014158:Transcription, Genetic
chemical_list: D012321:DNA-Directed RNA Polymerases