Key result
In vitro expression of the reovirus mu2 protein demonstrated non-sequence-specific RNA-binding activity that was enhanced in the presence of Mn2+ compared to Mg2+.
The reovirus protein μ2 is demonstrated to have non-sequence-specific RNA-binding activity, making it the sixth reovirus protein with this function.
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μ2 adds to reovirus RNA-binding proteins; leaves open its role in replication pending cellular and in vivo validation.
The reovirus M1, L1, and L2 genes encode proteins found at each vertex of the viral core and are likely to form a structural unit involved in RNA synthesis. Genetic analyses have implicated the M1 gene in viral RNA synthesis and core nucleoside triphosphatase activity, but there have been no direct biochemical studies of mu2 function. Here, we expressed mu2 in vitro and assessed its RNA-binding activity. The expressed mu2 binds both poly(I-C)- and poly(U)-Sepharose, and binding activity is greater in Mn2+ than in Mg2+. Heterologous RNA competes for mu2 binding to reovirus RNA transcripts as effectively as homologous reovirus RNA does, providing no evidence for sequence-specific RNA binding by mu2. Protein mu2 is now the sixth reovirus protein demonstrated to have RNA-binding activity.
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Brentano et al. (1998) studied this question. In vitro expression of mu2 protein was evaluated on RNA-binding activity. In vitro expression of the reovirus mu2 protein demonstrated non-sequence-specific RNA-binding activity that was enhanced in the presence of Mn2+ compared to Mg2+.
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