Genome-wide mapping of myosin protein-RNA networks suggests the existence of specialized protein production sites.

Motor proteins can organize posttranscriptional processes by transporting ribonucleoprotein complexes to specific locations. To investigate a possible role of myosin proteins in gene expression control, I have identified mRNAs associated with five myosin heavy chains in the fission yeast Schizosaccharomyces pombe, by purifying the proteins and identifying bound transcripts using DNA microarrays. Each myosin coimmunoprecipitated with 5-13 different mRNAs (approximately 0.1-0.2% of all genes), including those encoding four different myosin heavy chains. Moreover, one of the myosins (Myo1) interacted with mRNAs encoding components of the cortical actin cytoskeleton. These interactions were not observed in control immunoprecipitates. A myosin-specific chaperone (Rng3) that interacts cotranslationally with myosin mRNAs was essential for the association between myosin proteins and transcripts but not between Myo1 and other mRNAs. Finally, proteins encoded by the Myo1-associated mRNAs immunoprecipitated each other's transcripts, but not myosin mRNAs. These interactions suggest the existence of two distinct myosin-containing ribonucleoprotein complexes: those containing myosin mRNAs and those associated with Myo1. They are distinguished by their mRNA composition, requirement for the Rng3 chaperone and the presence of nonmyosin cytoskeletal proteins. I propose that these complexes represent specialized sites for the production of myosin proteins and the assembly of cytoskeletal components, respectively.