Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription

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Abstract
Actin is associated with all three nuclear RNA polymerases and acts in concert with nuclear myosin I (NM1) to drive transcription. Practically nothing is known regarding the state of actin and the functional interplay of actin and NM1 in transcription. Here we show that actin and NM1 act in concert to promote RNA polymerase I (Pol I) transcription. Drugs that prevent actin polymerization or inhibit myosin function inhibit Pol I transcription in vivo and in vitro. Mutants that stabilize the polymeric state actin are tightly associated with Pol I and activate transcription, whereas a polymerization-deficient mutant does not bind to Pol I and does not promote rDNA transcription. Consistent with nuclear actin and myosin synergizing in transcription activation, NM1 mutants that lack specific functions, such as binding to ATP, actin, or calmodulin, are incapable of associating with Pol I and rDNA. The results show that actin polymerization and the motor function of NM1 are required for association with the Pol I transcription machinery and transcription activation. These observations provide insights into the cooperative action of actin and myosin in the nucleus and reveal an actomyosin-based mechanism in transcription.