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1995 | 42 | 3 |

Tytuł artykułu

EF-1alpha is a target site for inhibitory effect of quercetin in the peptide elongation process

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The effect of quercetin (3,3',4',5,7-pentahydroxyflavone) on the polypeptide elon­gation system isolated from rat liver cells, was investigated. Quercetin inhibited [ 4C]leucine incorporation into proteins in vitro and the inhibitory effect is being directed towards the elongation factor eEF-1, but not to eEF-2 and ribosomes. Quer­cetin was found to form a complex with EF-la, which was inactive in GTP-dependent binding to ribosomes. It can be suggested that quercetin can block the total or the part of the domain of EF-la structure that is responsible for formation of the ternary complex EF-la-GTP-i14C]Phe-tRNA and therefore preventing formation of the quater­nary complex with ribosomes.

Wydawca

-

Rocznik

Tom

42

Numer

3

Opis fizyczny

p.347-350,fig.

Twórcy

  • Medical Academy, 15-230 Bialystok, Poland

Bibliografia

  • 1. Gajko, A., Sredzińska, K., Marcinkiewicz, C. & Gałasiński, W. (1991) The effect of phospho­rylation of the EF-2 isolated from rat liver cells on protein biosynthesis in vitro. Acta Biochim. Polon. 38,353-358.
  • 2. Gałasiński, W. & Moldave, K. (1969) Purification of a mi noacyl-transferase II (translocation fac­tor) from rat liver. /, Biol. Chem. 244, 6527-6532.
  • 3. Jabłonowska, K., Telejko, E., Kopacz-Jodczyk, T. & Gałasiński, W. (1981) Heterogeneous forms of elongation factor 1 (EF-1) from Guerin tumour cells in rats. I. Purification of EF-1A, EF-1B and EF-1C from Guerin tumour cells. Bull. Pol. Ac.: Biol. 29,361-366.
  • 4. Jabłonowska, K., Kopacz-Jodczyk, T., Nie- dźwiecka, J. & Gałasiński, W. (1983) Isolation and characterization of elongation factor EF-2 from Guerin tumour. Acta Biochim. Polon. 30, 381-388.
  • 5. Marcinkiewicz, C, Gajko, A. & Gałasiński, W. (1991) Purification and properties of the hete­rogeneous subunits of the elongation factor EF-1 from Guerin epithelioma cells. Acta Bio­chim. Polon. 38,129-134.
  • 6. Marcinkiewicz, C, Gajko, A. & Gałasiński, W. (1992) The phosphorylation of elongation factor EF-1 isolated from Guerin epithelioma. Acta Bio­chim. Polon. 39, 7-13.
  • 7. Marcinkiewicz, C. & Gałasiński, W. (1993) Isola­tion and properties of suburiit form EF-1C of elongation factor 1 from Guerin epithelioma cells. Acta Biochim. Polon. 40, 225-230.
  • 8. Średzińska, K., Gajko, A. & Gałasiński, W. (1991) Differences in the structures of the elongation factors (EF-2) isolated from Guerin epithelioma and rat liver. Bull. Pol. Ac.: Biol. 39,171-174.
  • 9. Telejko, E., Niedźwiecka, J., Łopaczyński, W., Zwierz, J. & Gałasiński, W. (1977) Characteri­zation of the elongation factors EF-1 and EF-2 from the tumour cells of the experimental Guerin epi­thelioma. (Nowak, H.F., ed.) pp. 46-50, Onko­logia Doświadczalna, Medical Academy Bia­łystok, (in Polish).
  • 10. Telejko, E., Jabłonowska, K., Skowroński, J. & Gałasiński, W. (1981) Heterogeneous forms of elongation factor 1 (EF-1) from Guerin tumour cells in rats. II. The character of highly purified heterogeneous forms of EF-1 isolated from Guerin tumour cells. Bull. Pol. Ac.: Biol. 29, 367-372.
  • 11. Yoshida, M., Yamamoto, M. & Nikaido, T. (1992) Quercetin arrests human leukemic T-cells in late Gi phase of the cell cycle. Cancer Res. 52,6676- -6681.
  • 12. Skogerson, L. & Moldave, K. (1969) The binding of ami noacyl transferase II to ribosomes. Bio- chem. Biophys. Res. Commun. 27, 568-572.
  • 13. Moldave, K. (1963) The preparation of C14-ami- noacyl soluble-tKNA. Methods Enzymol. 6, 757- -761.
  • 14. Cundliffe, E. (1968) Polyribosomes and riboso- mal sub-units of bacterial protoplasts. Biochem. Biophys. Res. Commun. 33,247-252.
  • 15. Vazquez, D. & Monro, R.E. (1967) Effects of some inhibitors of protein synthesis on the bin­ding of aminoacyl tRNA to ribosomal subunits. Biochim. Biophys. Acta 142,155-173.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-226218e6-49d5-43ae-afd1-47219618544e
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