The role of cholesteryl 14-methylhexadecanoate in the function of eukaryotic peptide elongation factor 1

1985 ◽  
Vol 146 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Zdena TUHACKOVA ◽  
Jan HRADEC
Keyword(s):  
Elongation Factor ◽  
Peptide Elongation ◽  
Elongation Factor 1

scholarly journals CTP can replace GTP in reactions catalyzed by eukaryotic peptide elongation factor 1

FEBS Letters ◽  
1984 ◽  
Vol 177 (1) ◽  
pp. 112-114 ◽  
Author(s):  
Z. Tuháčková ◽  
M. Havránek ◽  
J. Hradec
Keyword(s):  
Elongation Factor ◽  
Peptide Elongation ◽  
Elongation Factor 1

scholarly journals The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis

1987 ◽  
Vol 244 (2) ◽  
pp. 287-294 ◽  
Author(s):  
T G Obrig ◽  
T P Moran ◽  
J E Brown
Keyword(s):  
Protein Synthesis ◽  
Complex Formation ◽  
Shiga Toxin ◽  
Mode Of Action ◽  
Elongation Factor ◽  
Shigella Dysenteriae ◽  
Gtpase Activity ◽  
Elongation Factor 2 ◽  
Peptide Elongation ◽  
Elongation Factor 1

The effect of Shiga toxin, from Shigella dysenteriae 1, on the component reactions of peptide elongation were investigated. Enzymic binding of [3H]phenylalanine-tRNA to reticulocyte ribosomes was inhibited by 50% at 7 nM toxin. Elongation factor 1 (eEF-1)-dependent GTPase activity was also inhibited. Both reactions were not restored by addition of excess eEF-1 protein. In contrast, toxin concentrations of 200 nM were required to inhibit by 50% the elongation factor 2 (eEF-2)-dependent translocation of aminoacyl-tRNA on ribosomes. Addition of excess eEF-2 restored translocation activity. The eEF-2-dependent GTPase activity was unaffected at toxin concentrations below 100 nM, and Shiga-toxin concentrations of up to 1,000 nM did not affect either GTP.eEF-2.ribosome complex-formation or peptidyltransferase activity. Thus Shiga toxin closely resembles alpha-sarcin in action, both being primary inhibitors of eEF-1-dependent reactions. In contrast, the 60 S ribosome inactivators ricin and phytolaccin are primary inhibitors of eEF-2-dependent reactions of peptide elongation.

scholarly journals Evaluation on Elongation Factor 1 Alpha of Entamoeba histolytica Interaction with the Intermediate Subunit of the Gal/GalNAc Lectin and Actin in Phagocytosis

Pathogens ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 702
Author(s):  
Hang Zhou ◽  
Yue Guan ◽  
Meng Feng ◽  
Yongfeng Fu ◽  
Hiroshi Tachibana ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Chinese Hamster Ovary ◽  
Messenger Rna ◽  
Chinese Hamster ◽  
Elongation Factor ◽  
Elongation Factor 1 Alpha ◽  
Elongation Factor 1 ◽  
Pathogenic Process

Entamoeba histolytica is the causative agent of amoebiasis. This disease results in 40,000 to 100,000 deaths annually. The pathogenic molecules involved in the invasion of trophozoites had been constantly being clarified. This study explored the role of elongation factor 1 alpha (EF1a) in E. histolytica pathogenicity. Biolayer interferometry binding and pull-down assays suggest that EF1a and intermediate subunit of lectin (Igl) binding are specific. Submembranous distribution of EF1a closely aligns with the localization of Igl, which appear in abundance on membranes of trophozoites. Messenger RNA (mRNA) expression of EF1a is positively correlated with trends in Igl levels after co-incubation with Chinese hamster ovary (CHO) cells in vitro, suggesting a regulatory linkage between these proteins. Erythrophagocytosis assays also imply a role for EF1a in phagocytosis. Finally, EF1a and actin are collocated in trophozoites. These results indicated elongation factor 1a is associated with E. histolytica phagocytosis, and the relationships between EF1a, Igl, and actin are worth further study to better understand the pathogenic process.

scholarly journals Peptide elongation in rat kidney after cadmium administration

1980 ◽  
Vol 190 (3) ◽  
pp. 791-797 ◽  
Author(s):  
M J Kuliszewski ◽  
D M Nicholls
Keyword(s):  
Rat Kidney ◽  
Gel Filtration ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Renal Tissue ◽  
Elongation Factors ◽  
Elongation Factor 2 ◽  
Peptide Elongation ◽  
Elongation Factor 1 ◽  
Trna Binding

Rats received two injections (each 2.6 mg/kg body wt.) of CdCl2, and the kidneys were removed 24 h later. Postmicrosomal supernatant fractions of the homogenized kidneys were used as a source of elongation factors 1 and 2 in assays for [14C]phenylalanyl-tRNA binding to ribosomes and for peptide-bond synthesis. After purification of these preparations by precipitation with (NH4)2SO4 and gel filtration on Sephadex G-200 and G-100, elongation factor 1 activity was significantly increased. A significant increase in the activity of purified elongation factor 2 was also found. The results are discussed in relation to the reported effects of CdCl2 and of HgCl2 on renal tissue.

scholarly journals Role of Phospholipids in the Multiple Forms of Mammalian Elongation Factor 1

1974 ◽  
Vol 71 (6) ◽  
pp. 2179-2182 ◽  
Author(s):  
A. B. Legocki ◽  
B. Redfield ◽  
C. K. Liu ◽  
H. Weissbach
Keyword(s):  
Elongation Factor ◽  
Multiple Forms ◽  
Elongation Factor 1

scholarly journals In vivo characterization of the role of tissue‐specific translation elongation factor 1 A 2 in protein synthesis reveals insights into muscle atrophy

FEBS Journal ◽  
2013 ◽  
Vol 280 (24) ◽  
pp. 6528-6540 ◽  
Author(s):  
Jennifer Doig ◽  
Lowri A. Griffiths ◽  
David Peberdy ◽  
Permphan Dharmasaroja ◽  
Maria Vera ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Atrophy ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
In Vivo Characterization ◽  
Elongation Factor 1

scholarly journals Isolation and properties of the subunit form EF-1C of elongation factor 1 from Guerin epithelioma cells.

1993 ◽  
Vol 40 (2) ◽  
pp. 225-230
Author(s):  
C Marcinkiewicz ◽  
W Gałasiński
Keyword(s):  
Molecular Mass ◽  
Thermal Sensitivity ◽  
Elongation Factor ◽  
Protective Role ◽  
Eukaryotic Cells ◽  
Active Complex ◽  
Elongation Factor 1

EF-1C is a component of the aggregate EF-1B, consisting of the subunit forms EF-1A.EF-1C; it was isolated by dissociation of this aggregate in the presence of GTP. The subunit form EF-1C stimulates binding of aminoacyl-tRNA to ribosomes, catalysed by EF-1A, similarly as EF-1 beta gamma which stimulates the activity of EF-1 in other eukaryotic cells. EF-1C in the presence of 6 M urea was separated into two polypeptides. Polypeptide of molecular mass 32,000 Da is responsible for regeneration of the EF-1A.GTP active complex. Thermal sensitivity of EF-1A was much higher than that of EF-1B, thus a protective role of EF-1C in the EF-1A.EF-1C complex is suggested.

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