Abstract
Transfer RNA-mediated posttranslational protein modification by arginine has been demonstrated in vitro in axoplasm extruded from the giant axons of squid and in injured and regenerating vertebrate nerves. In nerve and axoplasm, the highest activity is found in a fraction of a 150,000 × g supernatant containing high molecular weight protein/RNA complexes but lacking molecules of <5 kDa. Arginylation (and protein modification by other amino acids) is not found in more purified, reconstituted fractions. The data are interpreted as indicating that it is critical to recover the reaction components in high molecular weight protein/RNA complexes in order to maintain maximum physiological activity. The level of arginylation is greatest in injured and growing vertebrate nerves compared with intact nerves, suggesting a role for these reactions in nerve injury/repair and during axonal growth.
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References
Lasek RJ, Dabrowski C, Nordlander R (1973) Analysis of axoplasmic RNA from invertebrate giant axons. Nat New Biol 244(136):162–165
Black MM, Lasek RJ (1977) The presence of transfer RNA in the axoplasm of the squid giant axon. J Neurobiol 8(3):229–237
Ingoglia NA, Giuditta A, Zanakis MF, Babigian A, Tasaki I, Chakraborty G, Sturman JA (1983) Incorporation of 3H-amino acids into proteins in a partially purified fraction of axoplasm: evidence for transfer RNA-mediated, post-translational protein modification in squid giant axons. J Neurosci 3(12):2463–2473
Ingoglia NA (1979) 4S RNA is present in regenerating optic axons of goldfish. Science 206(4414):73–75
Lindquist TD, Ingoglia NA, Gould RM (1981) 4S RNA is transported axonally in normal and regenerating axons of the sciatic nerves of rats. Brain Res 230(1-2):181–194
Sotelo-Silveira JR, Holt CE (2014) Introduction to the special issue on local protein synthesis in axons. Dev Neurobiol 74(3):207–209
Zanakis MF, Chakraborty G, Sturman JA, Ingoglia NA (1984) Posttranslational protein modification by amino acid addition in intact and regenerating axons of the rat sciatic nerve. J Neurochem 43(5):1286–1294
Baker PF, Schlaepfer WW (1978) Uptake and binding of calcium by axoplasm isolated from giant axons of Loligo and Myxicola. J Physiol 276:103–125
Metuzals J (1969) Configuration of a filamentous network in the axoplasm of the squid (Loligo pealei L.) giant nerve fiber. J Cell Biol 43(3):480–505
Espinoza-Lewis RA, Wang DZ (2012) MicroRNAs in heart development. Curr Top Dev Biol 100:279–317
Zalts H, Shomron N (2011) The impact of microRNAs on endocrinology. Pediatr Endocrinol Rev 8(4):354–362, quiz 362–3
Boss IW, Renne R (2011) Viral miRNAs and immune evasion. Biochim Biophys Acta 1809(11-12):708–714
Kwak PB, Iwasaki S, Tomari Y (2010) The microRNA pathway and cancer. Cancer Sci 101(11):2309–2315
Yang M, Li Y, Padgett RW (2005) MicroRNAs: small regulators with a big impact. Cytokine Growth Factor Rev 16(4-5):387–393
Starega-Roslan J, Koscianska E, Kozlowski P, Krzyzosiak WJ (2011) The role of the precursor structure in the biogenesis of microRNA. Cell Mol Life Sci 68(17):2859–2871
Lehrbach NJ, Miska EA (2010) Regulation of pre-miRNA processing. Adv Exp Med Biol 700:67–75
Sasaki Y, Gross C, Xing L, Goshima Y, Bassell GJ (2014) Identification of axon-enriched microRNAs localized to growth cones of cortical neurons. Dev Neurobiol 74(3):397–406
Iyer AN, Bellon A, Baudet ML (2014) MicroRNAs in axon guidance. Front Cell Neurosci 8:78
Yu M, Chakraborty G, Grabow M, Ingoglia NA (1994) Serine protease inhibitors block N-terminal arginylation of proteins by inhibiting the arginylation of tRNA in rat brains. Neurochem Res 19(1):105–110
Yu M, Grabow M, Ingoglia NA (1993) Isolation of a peptide that inhibits the posttranslational arginylation of proteins in rat brain. J Mol Neurosci 4(3):195–203
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Ingoglia, N.A. (2015). Arginylation in a Partially Purified Fraction of 150k × g Supernatants of Axoplasm and Injured Vertebrate Nerves. In: Kashina, A. (eds) Protein Arginylation. Methods in Molecular Biology, vol 1337. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2935-1_4
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DOI: https://doi.org/10.1007/978-1-4939-2935-1_4
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-2934-4
Online ISBN: 978-1-4939-2935-1
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