RNA-enzyme interactions are at the heart of many fundamental biological processes such as transcription, translation, and RNA silencing. Determination of the thermodynamics and kinetics of these interactions is crucial for the understanding of cellular and viral biology.We have applied single-molecule magnetic tweezers (MT) to study transcription kinetics of RNA-dependent RNA polymerase from Bacteriophage Φ6 (Φ6 RdRP). During transcription RdRP binds to the antisense strand of the double-stranded RNA genome and polymerases a new sense strand while displacing the old one. In vivo, this reaction is repeated many a times to generate a pool of sense strands that are translated by the host to generate viral proteins.In MT sense strand was suspended between glass surface and a paramagnetic bead and hybridized to its complementary antisense strand to form dsRNA. AsΦ6 RdRP progresses along the antisense strand it unwinds dsRNA releasing the sense strand in a single-stranded form. The rate of this release was measured with MTs and used to analyze the transcription kinetics.During a single round of transcription, Φ6 RdRP switches between a moving state and a pause state. We could show that the overall rate (i.e. including the moving and pause states) depends on the applied force while the instantaneous rate (i.e. including only the moving state) reveals no force dependence. Likewise the pause frequency does not show any force dependence while the analysis of pause duration demonstrated that the exit from the pause state is slower at forces below 15 pN. We have analyzed the obtained results in the context of RNA-enzyme interaction as well as Φ6 RdRP's unwinding ability.