The dynamic machinery of mRNA elongation.
Two complementary X-ray studies of the interaction between RNA polymerase II and nucleic acids have improved our understanding of mRNA elongation. These studies suggest how RNA polymerase II unwinds DNA, how it separates the RNA product from the DNA template and how it incorporates nucleoside triphosphate (NTP) substrates into the growing RNA chain. The tunable polymerase active center apparently allows repositioning of a catalytic metal ion, rotation of NTPs before their incorporation, RNA repositioning by a transcript cleavage factor, and modulation of enzyme activity by a bacterial small molecule regulator and its protein cofactor.
Armache
Karim-Jean
KJ
Department of Chemistry and Biochemistry, Gene Center, Ludwig-Maximilians-University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.
Kettenberger
Hubert
H
Cramer
Patrick
P
D002384:Catalysis; D004247:DNA / Q000737:chemistry*; D007700:Kinetics; D009690:Nucleic Acid Conformation; D009705:Nucleosides / Q000737:chemistry*; D012319:RNA Polymerase II / Q000737:chemistry*; D012333:RNA, Messenger / Q000737:chemistry*; D013329:Structure-Activity Relationship; D015533:Transcriptional Activation; D035602:Transcriptional Elongation Factors / Q000737:chemistry*
D009705:Nucleosides; D012333:RNA, Messenger; D035602:Transcriptional Elongation Factors; D004247:DNA; D012319:RNA Polymerase II