She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p.

RNA localization is a widespread mechanism to achieve localized protein synthesis. In budding yeast, localization of ASH1 mRNA controls daughter cell-specific accumulation of the transcriptional regulator Ash1p, which determines mating type switching. ASH1 mRNA localization depends on four independently acting sequences ('zipcodes') within the mRNA. In addition, the class V ...
myosin Myo4p and a set of She proteins with as yet unknown function are essential for ASH1 localization. Here we show that She2p is a novel RNA-binding protein that binds specifically to ASH1 mRNA in vivo and to ASH1 RNA zip codes in vitro. She2p can interact with She3 protein via She3p's C-terminus and becomes localized to the daughter cell tip upon ASH1 expression. The N-terminal coiled-coil domain of She3p is required to form an RNA-independent complex with the heavy chain of the myosin motor protein Myo4p. She2p and She3p are the first examples of adapters for tethering a localized mRNA to the motor protein and might serve as prototypes for RNA-motor protein adapters.
Mesh Terms:
DNA-Binding Proteins, Fluorescent Antibody Technique, Fungal Proteins, In Situ Hybridization, Myosin Heavy Chains, Myosin Type V, Myosins, Nucleic Acid Conformation, Precipitin Tests, Protein Binding, RNA, Fungal, RNA, Messenger, RNA-Binding Proteins, Recombinant Fusion Proteins, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors, Two-Hybrid System Techniques
EMBO J.
Date: Oct. 16, 2000
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