Abstract
Polyamines exist mainly as RNA–polyamine complexes in cells. Thus, we looked for proteins whose synthesis is enhanced by polyamines at the level of translation in mammalian cells. Here, we describe how synthesis of Cct2 (T-complex protein 1, β-subunit, a chaperonin assisting in the folding actin, tubulin, and several other proteins) and eEF1A (one of the elongation factors of protein synthesis) is stimulated by polyamines at the level of translation. Polyamines stimulated Cct2 synthesis through the stimulation of ribosome shunting during 5′-processive scanning of 40S ribosomal subunits from the m7G-cap to the initiation codon AUG, and eEF1A synthesis through the structural change of the unusual position of a complementary sequence to 18S rRNA in eEF1A mRNA.
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We are grateful to Dr. A.J. Michael for critical reading of the manuscript prior to submission.
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Kashiwagi, K., Terui, Y., Igarashi, K. (2018). Modulation of Protein Synthesis by Polyamines in Mammalian Cells. In: Alcázar, R., Tiburcio, A. (eds) Polyamines. Methods in Molecular Biology, vol 1694. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7398-9_27
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DOI: https://doi.org/10.1007/978-1-4939-7398-9_27
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