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

100%

Marcinkiewicz C. , Galasinski W. , Gindzienski A.

Acta Biochimica Polonica

1995

tom 42

nr 3

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.

Differences in the structures of the elongation factors (EF-2) isolated from guerin epithelioma and rat liver

75%

Sredzinska K. , Gajko A. , Galasinski W.

1991

tom 39

nr 2

The phosphorylation of elongation factor EF-1 isolated from guerin epithelioma

75%

Marcinkiewicz C. , Gajko A. , Galasinski W.

Acta Biochimica Polonica

1992

tom 39

nr 1

Evidence for plant ribosomal 5S RNA involvement in elongation of polypeptide chain biosynthesis

63%

Shaikhin S. , Sobkiewicz A. , Barciszewski J. , Twardowski T.

1994

tom 41

nr 1

A series of short oligo-DNA probes (8-10-mers) complementary to various regions of the plant ribosomal 5S ribonucleic acid (5S rRNA) have been synthesized. The results of their hybridization to free 5S rRNA and to ribosomes pointed to the availability of nucleotides in loop "C" for complexation. We found a correlation between hybridization of selected oligonucleotides and their inhibitory effect on enzymatic binding of Phe-tRNA and poly(Phe) synthesis on wheat germ 80S ribosomes. Evidence was obtained for involvement of 5S rRNA in the elongation of polypeptide chain during protein biosynthesis. 5S rRNA seems to play a critical role in protein biosynthesis, probably through causing conformational changes of loop C.

Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells

63%

Gajko A. , Galasinski W. , Gindzienski A.

1994

tom 41

nr 4

The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electTophoretically homogeneous protein with relative molecular mass of approximately 90000 and isoelectric point, pi = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.

Zaleznosc miedzy masa bulw odmian jadalnych a ich wymiarami i ksztaltem

51%

Zarzynska K.

1993

nr 43

57-63