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      The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p.

      Proceedings of the National Academy of Sciences of the United States of America
      Binding Sites, Carrier Proteins, isolation & purification, metabolism, DNA-Binding Proteins, Fungal Proteins, Models, Biological, Myosin Heavy Chains, Myosin Type V, Myosins, RNA, Fungal, genetics, RNA, Messenger, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors, Zinc Fingers

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          Abstract

          In Saccharomyces cerevisiae, mRNA encoding the cell-fate determinant Ash1p is localized to the distal tip of daughter cells. Five SHE genes are required for proper Ash1 mRNA localization, one of which encodes the myosin Myo4p. We show that three of the five She proteins, She2p, She3p, and Myo4p, colocalize with Ash1 mRNA in vivo and coimmunoprecipitate with Ash1 mRNA from cell extracts. We also find that She3p binds to Myo4p in the absence of RNA and She2p is required for binding She3p-Myo4p to Ash1 mRNA. These results suggest that She3p acts as an adapter protein that docks the myosin motor onto an Ash1-She2p ribonucleoprotein complex.

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