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      The cauliflower mosaic virus translational transactivator interacts with the 60S ribosomal subunit protein L18 of Arabidopsis thaliana.

      Biology
      Amino Acid Sequence, Arabidopsis, metabolism, virology, Caulimovirus, genetics, Cloning, Molecular, Molecular Sequence Data, Phosphorylation, Plant Leaves, Plant Proteins, chemistry, Protein Biosynthesis, Ribosomal Proteins, Sequence Analysis, DNA, Trans-Activators, Transcriptional Activation, Viral Proteins

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          Abstract

          The cauliflower mosaic virus (CaMV) open reading frame VI product (P6) is involved in several aspects of the infectious cycle. P6 specifically controls the synthesis of other CaMV proteins by transactivating their expression from the polycistronic 35S RNA. By far-Western assays, we have demonstrated that P6 interacts with proteins from both healthy and CaMV-infected leaves of Arabidopsis thaliana. These proteins are found in ribosome-enriched extracts, suggesting that they participate in the translation process. One of these proteins, identified by microsequencing, corresponds to the 60S ribosomal subunit protein L18 (RPL18). Its cDNA was cloned and expressed in Escherichia coli, and the resulting RPL18 protein was shown to interact with the minimal region required for translational transactivation, designated the miniTAV domain of P6. Copyright 2000 Academic Press.

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