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The role of elongation factors in protein synthesis rate variation in white teleost muscle

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Summary

Protein synthesis-stimulating activity was assayed in the cytosolic fraction of white muscle from teleost fish (rainbow trout, carp) and of rat liver. In vitro protein synthesis-stimulating activity in the cytosolic fraction is reduced by food deprivation. The addition of elongation factors EF1, EF2, or EF1+EF2 compensates for the starvation-induced loss of protein synthesis-stimulating activity in trout muscle cytosol. The action of EF2 is stronger than that of EF1 in this respect. However, EF1 enhances in vitro protein synthesis-stimulating activity in rat liver cytosol more than EF2. The EF2 concentration in the cytosolic fraction of white muscle from starved trout is significantly lower than in fed specimens.

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Abbreviations

EF:

elongation factor(s)

SGR:

specific growth rate

TCA:

trichloroacetic acid

References

  • Bommer U-A, Junghahn I, Bielka H (1987) The role of the cytosolic fraction and of initiation factor eIF-2 for changes of the rate of protein synthesis during liver regeneration. Biol Chem Hoppe Seyler 368:445–450

    Google Scholar 

  • Decken A von der (1983) Experimental studies on the quality of food proteins. Comp Biochem Physiol 74B:213–220

    Google Scholar 

  • Fauconneau B (1985) Protein synthesis and protein deposition in fish. In: Cowey CB, Mackie AM, Bell JG (eds) Fish nutrition. Academic Press, London, pp 17–45

    Google Scholar 

  • Haschemeyer AEV (1978) Protein metabolism and its role in temperature acclimation. In: Malins DC, Sargent JR (eds) Biochemical and biophysical perspectives in marine biology, vol 4. Academic Press, London New York San Francisco, pp 29–84

    Google Scholar 

  • Honjo T, Nishizuka Y, Hayashi O, Kato I (1968) Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis. J Biol Chem 243:3553–3555

    Google Scholar 

  • Huisman EAC (1976) Food conversion efficiencies at maintenance and production levels for carp, Cyprinus carpio L., and rainbow trout, Salmo gairdneri Richardson. Aquaculture 9:259–273

    Google Scholar 

  • Junghahn I, Jürss K (1988) Effects of feeding and salinity on protein synthesis in the white epaxial muscle of the rainbow trout (Salmo gairdneri Richardson). Comp Biochem Physiol 89B:329–333

    Google Scholar 

  • Junghahn I, Scholz I (1973) Isolierung und einige Eigenschaften von Polysomen aus Rattenleber. Acta Biol Med Ger 31:691–699

    Google Scholar 

  • Junghahn I, Jürss K, Bastrop R (1989) Activity of cytosolic fraction from rainbow trout muscle to stimulate polysomal protein synthesis in relation to dietary changes and environmental salinity. Zool Jahrb Abt Allg Zool Physiol Tiere 93:417–423

    Google Scholar 

  • Lied E, Lund B, von der Decken A (1982) Protein synthesis in vitro by epaxial muscle polyribosomes from cod, Gadus morhua. Comp Biochem Physiol 72B:187–193

    Google Scholar 

  • Lied E, Rosenlund G, Lund B, von der Decken A (1983) Effect of starvation and refeeding on in vitro protein synthesis in white trunk muscle of Atlantic cod (Gadus morhua). Comp Biochem Physiol 76B:777–781

    Google Scholar 

  • Loughna PT, Goldspink G (1984) The effects of starvation upon protein turnover in red and white myotomal muscle of rainbow trout, Salmo gairdneri Richardson. J Fish Biol 25:223–230

    Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin-phenol reagent. J Biol Chem 193:265–275

    CAS  PubMed  Google Scholar 

  • Lund B, von der Decken A (1980) Protein synthesis in vitro after cryopreservation of rat skeletal muscle. Z Tierphysiol Tierernähr Futtermittelkd 44:255–266

    Google Scholar 

  • McCarthy JEG, Gualerzi CO (1990) Translational control of procaryotic gene expression. Trends in Genetics 6:78–85

    Google Scholar 

  • Millward DJ (1989) The nutritional regulation of muscle growth and protein turnover. Aquaculture 79:1–28

    Google Scholar 

  • Moldave K (1985) Eucaryotic protein synthesis. Ann Rev Biochem 54:1109–1149

    Google Scholar 

  • Moldave K (1990) Discovery, purification, and function of elongation factors. In: Deutscher MP (ed) Guide in protein purification (Methods in enzymology, vol 182). Academic Press, San Diego, pp 809–818

    Google Scholar 

  • Nielsen JBK, Plant PW, Haschemeyer AEV (1977) Control of protein synthesis in temperature acclimation. II. Correlation of elongation factor 1 activity with elongation rate in vivo. Physiol Zool 50:22–30

    Google Scholar 

  • Noll F, Heumann W, Littmann G (1966) Methode zur Darstellung reinster myokinasefreier Pyruvatkinase aus Kaninchenmuskel. Acta Biol Med Ger 16:115–121

    Google Scholar 

  • Rasch D, Enderlein G, Herrendörfer G (1973) Biometrie, Verfahren, Tabellen, angewandte Statistik. VEB Deutscher Landwirtschaftsverlag, Berlin

    Google Scholar 

  • Riis B, Rattan SIS, Clark BFC, Merrick WC (1990) Eucaryotic protein elongation factors. Trends Biochem Sci 15:420–424

    Google Scholar 

  • Roels-De Schrijver MP (1985) Influence of fasting and refeeding on the elongation step protein synthesis in rat liver of young (3M) and aging (18 M) animals. Exp Gerontol 20:193–200

    Google Scholar 

  • Rosenlund G, Lied E (1986) Growth and muscle protein synthesis in vitro of saithe (Pollachius virens) and rainbow trout (Salmo gairdneri) in response to protein-energy intake. Acta Agric Scand 36:195–204

    Google Scholar 

  • Rosenlund G, Lund B, Sandnes K, Braekkan OR, von der Decken A (1984) Muscle protein synthesis in vitro of saithe (Pollachius virens) correlated to growth and daily energy intake. Comp Biochem Physiol 77B:7–13

    Google Scholar 

  • Ryazanov AG (1987) Ca2+/calmodulin-dependent phosphorylation of elongation factor 2. FEBS Lett 214:331–334

    Google Scholar 

  • Ryazanov AG, Ovchinnikov LP, Spirin AS (1987) Development of structural organization of protein-synthesizing machinery from procaryotes to eucaryotes. Biosystems 20:275–288

    Google Scholar 

  • Sidell BC (1977) Turnover of cytochrome c in skeletal muscle of green sunfish (Lepomis cyanellus R.) during thermal acclimation. J Exp Zool 199:233–250

    Google Scholar 

  • Simon E (1987) Effect of acclimation temperature on the elongation step of protein synthesis in different organs of rainbow trout. J Comp Physiol B 157:201–207

    Google Scholar 

  • Sitikov AS, Simonenko PN, Shestakova EA, Ryazanov AG, Ovchinnikov LP (1988) cAMP-dependent activation at protein synthesis correlates with dephosphorylation of the elongation factor 2. FEBS Lett 228:327–331

    Google Scholar 

  • Smith MAK (1981) Estimation of growth potential by measurement of tissue protein synthetic rates in feeding and fasting rainbow trout, Salmo gairdneri Richardson. J Fish Biol 19:213–220

    Google Scholar 

  • Somero G (1983) Environmental adaptation of proteins: strategies for the conservation of critical functional and structural traits. Comp Biochem Physiol 76A:621–633

    Google Scholar 

  • Van Ness BG, Howard JB, Bodley JW (1978) Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin modified yeast elongation factor 2. J Biol Chem 253:8687–8690

    Google Scholar 

  • Van Ness BG, Howard JB, Bodley JW (1980) ADP-ribosylation of elongation factor 2 by diphtheria toxin. J Biol Chem 255:10710–10716

    Google Scholar 

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Authors and Affiliations

  1. Department of Animal Physiology, University of Rostock, Universitätsplatz 2, O-2500, Rostock 1, FRG

    Karl Jürss & Ralf Bastrop

  2. Central Institute of Molecular Biology, O-1115, Berlin-Buch, FRG

    Ilse Junghahn

Authors
  1. Karl Jürss
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  2. Ilse Junghahn
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  3. Ralf Bastrop
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Jürss, K., Junghahn, I. & Bastrop, R. The role of elongation factors in protein synthesis rate variation in white teleost muscle. J Comp Physiol B 162, 345–350 (1992). https://doi.org/10.1007/BF00260762

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