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Hold on!: RNA polymerase interactions with the nascent RNA modulate transcription elongation and termination Grohmann D; Werner FRNA Biol 2010[May]; 7 (3): 310-5Evolutionary related multisubunit RNA polymerases from all three domains of life, Eukarya, Archaea and Bacteria, have common structural and functional properties. We have recently shown that two RNAP subunits, F/E (RPB4/7)-which are conserved between eukaryotes and Archaea but have no bacterial homologues-interact with the nascent RNA chain and thereby profoundly modulate RNAP activity. Overall F/E increases transcription processivity, but it also stimulates transcription termination in a sequence-dependent manner. In addition to RNA-binding, these two apparently opposed processes are likely to involve an allosteric mechanism of the RNAP clamp. Spt4/5 is the only known RNAP-associated transcription factor that is conserved in all three domains of life, and it stimulates elongation similar to RNAP subunits F/E. Spt4/5 enhances processivity in a fashion that is independent of the nontemplate DNA strand, by interacting with the RNAP clamp. Whereas the molecular mechanism of Spt4/5 is universally conserved in evolution, the added functionality of F/E-like complexes has emerged after the split of the bacterial and archaeoeukaryotic lineages. Interestingly, bacteriophage-encoded antiterminator proteins could, in theory, fulfil an analogous function in the bacterial RNAP.|*Transcription, Genetic/genetics/physiology[MESH]|Animals[MESH]|DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism/physiology[MESH]|Humans[MESH]|Models, Biological[MESH]|Models, Molecular[MESH]|Peptide Chain Termination, Translational/*physiology[MESH]|Protein Binding/physiology[MESH]|RNA/*metabolism[MESH]|Transcription Initiation Site[MESH]|Transcriptional Elongation Factors/metabolism[MESH] |
