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Abstract
Puralpha, which is involved in diverse aspects of cellular functions, is strongly expressed in neuronal cytoplasm. Previously, we have reported that this protein controls BC1 RNA expression and its subsequent distribution within dendrites and that Puralpha is associated with polyribosomes. Here, we report that, following treatment with EDTA, Puralpha was released from polyribosomes in mRNA/protein complexes (mRNPs), which also contained mStaufen, Fragile X Mental Retardation Protein (FMRP), myosin Va, and other proteins with unknown functions. As the coimmunoprecipitation of these proteins by an anti-Puralpha antibody was abolished by RNase treatment, Puralpha may assist mRNP assembly in an RNA-dependent manner and be involved in targeting mRNPs to polyribosomes in cooperation with other RNA-binding proteins. The immunoprecipitation of mStaufen- and FMRP-containing mRNPs provided additional evidence that the anti-Puralpha detected structurally or functionally related mRNA subsets, which are distributed in the somatodendritic compartment. Furthermore, mRNPs appear to reside on rough endoplasmic reticulum equipped with a kinesin motor. Based on our present findings, we propose that this rough endoplasmic reticulum structure may form the molecular machinery that mediates and regulates multistep transport of polyribosomes along microtubules and actin filaments, as well as localized translation in the somatodendritic compartment.
Highlights
We reported that the single-stranded DNA- and RNA-binding protein Pur␣, which is involved in the control of DNA replication, transcription, and translation (1), has the dual ability to up-regulate transcription of the BC1 RNA gene (2) and to mediate subsequent distribution of BC1 RNA within the somatodendritic compartment (3)
We demonstrated that mStaufen, Fragile X Mental Retardation Protein (FMRP), and myosin Va, which play a role in mRNA transport and translation, are coimmunoprecipitated with Pur␣/polyribosome complexes (Fig. 3B)
As the immunoprecipitation of these proteins by an anti-Pur␣ antibody was abolished by treatment with RNase A (Fig. 6), Pur␣ may play a role in the assembly of these large mRNA/protein complexes (mRNPs) in an RNA-dependent manner
Summary
We reported that the single-stranded DNA- and RNA-binding protein Pur␣, which is involved in the control of DNA replication, transcription, and translation (1), has the dual ability to up-regulate transcription of the BC1 RNA gene (2) and to mediate subsequent distribution of BC1 RNA within the somatodendritic compartment (3). Little is known about when and where these polyribosomes are formed and how they emerge at postsynaptic sites, RNA-binding proteins that associate with polyribosomes appear to be involved These proteins include mammalian Staufen (mStaufen) (8, 9), Embryonic Lethal Abnormal Vision (ELAV/ Hu) (10), and Fragile X Mental Retardation Protein (FMRP) (11, 12). It is possible that Pur␣ may serve a distinct function in gene expression at the cytoplasmic level via RNAs that contain such consensus sequences. In this context, it would be intriguing to characterize the proteins that interact with Pur␣-polyribosome complexes. MRNP with Pur␣, mStau, FMRP, and Myo Va and Its Transport diates and regulates dendritic transport and localized translation of mRNAs in polyribosomes
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