Abstract
Polyamines mainly exist as an RNA–polyamine complex in cells. Thus, the effects of polyamines on protein synthesis were examined in Escherichia coli, Saccharomyces cerevisiae, and mouse mammary carcinoma cells. It was found that several kinds of protein synthesis, which are involved in cell growth and viability, were stimulated by polyamines at the level of translation. We proposed that a set of genes whose expression is enhanced by polyamines at the level of translation can be classified as a “polyamine modulon.” Thus far, 17 kinds of genes in E. coli and 4 kinds of genes in eukaryotes were identified as members of polyamine modulon. There are several mechanisms underlying polyamine stimulation of protein synthesis in E. coli. First, polyamines stimulated several kinds of protein synthesis when a Shine–Dalgarno (SD) sequence in the mRNAs is distant from the initiation codon AUG. Second, polyamines stimulated an inefficient initiation codon UUG- or GUG-dependent fMet-tRNA binding to ribosomes. Third, polyamines stimulated read-through of the amber codon UAG by Gln-tRNASupE or +1 frameshifting at the termination codon UGA on the open reading frame. In eukaryotes, polyamines stimulated ribosome shunting during the scanning of the Met-tRNAi-40S ribosomal subunit complex from the cap structure to the initiation codon AUG of mRNAs.
Keywords
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Higashi K, Terui Y, Suganami A et al (2008) Selective structural change by spermidine in the bulged-out region of double-stranded RNA and its effect on RNA function. J Biol Chem 283:32989–32994
Igarashi K, Kashiwagi K (2010) Modulation of cellular function by polyamines. Int J Biochem Cell Biol 42:39–51
Kusama-Eguchi K, Watanabe S, Irisawa M et al (1991) Correlation between spermine stimulation of rat liver Ile-tRNA formation and structural change of the acceptor stem by spermine. Biochem Biophys Res Commun 177:745–750
Miyamoto S, Kashiwagi K, Ito K et al (1993) Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli. Arch Biochem Biophys 300:63–68
Nishimura K, Murozumi K, Shirahata A et al (2005) Independent roles of eIF5A and polyamines in cell proliferation. Biochem J 385:779–785
Nishimura K, Okudaira H, Ochiai E et al (2009) Identification of proteins whose synthesis is preferentially enhanced by polyamines at the level of translation in mammalian cells. Int J Biochem Cell Biol 41:2251–2261
Park MH, Nishimura K, Zanelli CF, Valentini SR (2010) Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids 38:491–500
Pegg AE (2009) Mammalian polyamine metabolism and function. IUBMB Life 61:880–894
Quigley GJ, Teeter MM, Rich A (1978) Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc Natl Acad Sci USA 75:64–68
Sakamoto A, Terui Y, Yamamoto T et al (2012) Enhanced biofilm formation and/or cell viability by polyamines through stimulation of response regulators UvrY and CpxR in the two-component signal transducing systems, and ribosome recycling factor. Int J Biochem Cell Biol 44:1877–1886
Su X, Dowhan W (2006) Translational regulation of nuclear gene COX4 expression by mitochondrial content of phosphatidylglycerol and cardiolipin in Saccharomyces cerevisiae. Mol Cell Biol 26:743–753
Terui Y, Tabei Y, Akiyama M et al (2010) Ribosome modulation factor, an important protein for cell viability encoded by the polyamine modulon. J Biol Chem 285:28698–28707
Terui Y, Akiyama M, Sakamoto A et al (2012) Increase in cell viability by polyamines through stimulation of the synthesis of ppGpp regulatory protein and ω protein of RNA polymerase in Escherichia coli. Int J Biochem Cell Biol 44:412–422
Uemura T, Higashi K, Takigawa M et al (2009) Polyamine modulon in yeast: stimulation of COX4 synthesis by spermidine at the level of translation. Int J Biochem Cell Biol 41:2538–2545
Wada A, Igarashi K, Yoshimura S et al (1995) Ribosome modulation factor: stationary growth phase-specific inhibitor of ribosome functions from Escherichia coli. Biochem Biophys Res Commun 214:410–417
Watanabe S, Kusama-Eguchi K, Kobayashi H, Igarashi K (1991) Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver. J Biol Chem 266:20803–20809
Yoshida M, Kashiwagi K, Shigemasa A et al (2004) A unifying model for the role of polyamines in bacterial cell growth, the polyamine modulon. J Biol Chem 279:46008–46013
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer Japan
About this chapter
Cite this chapter
Igarashi, K., Terui, Y., Kashiwagi, K. (2015). The Polyamine Modulon: Genes Encoding Proteins Whose Synthesis Is Enhanced by Polyamines at the Level of Translation. In: Kusano, T., Suzuki, H. (eds) Polyamines. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55212-3_11
Download citation
DOI: https://doi.org/10.1007/978-4-431-55212-3_11
Published:
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-55211-6
Online ISBN: 978-4-431-55212-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)