NDLI: Mitochondrial Poypeptide Elongation Factor EF-Tu of Saccharomyces cerevisiae. Functional and Structural Homologies to Escherichia coli EF-Tu

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Mitochondrial Poypeptide Elongation Factor EF-Tu of Saccharomyces cerevisiae. Functional and Structural Homologies to Escherichia coli EF-Tu

Content Provider	Scilit
Author	Piechulla, Birgit Kuntzel, Hans
Copyright Year	1983
Description	Journal: Journal of Biological Inorganic Chemistry The polypeptide elongation factor EF-Tu was isolated from a mitochondrial 100 000 x g supernatant of the yeast Saccharomyces cerevisiae and purified over 880-fold by DEAE-Sephadex chromatography and gel filtration. The factor efficiently replaces bacterial EF-Tu in a phenylalanine polymerizing cell-free system of Escherichia coli, it binds GDP and it protects phenylalanyl-tRNA against hydrolysis of the ester bond in the presence of 10 mM GTP. The polymerizing activity of the mitochondrial factor is inhibited to 90% by 50 microM N-ethylmaleimide and to 50% by 2.5 microM kirromycin. The purified factor contains two major polypeptides of apparent molecular weights 48 000 and 34 000. Antibodies raised against the 48 000-Mr protein react with EF-TuE. coli, as revealed by immune blotting and by the inhibition of phenylalanine polymerization. No reaction was observed between anti-(34 000-Mr) and 48 000-Mr protein or EF-TuE. coli. The 48 000-Mr protein has the same isoelectric point (pI = 6.2) and a content of cysteine and basic amino acids similar to the bacterial EF-Tu. It is concluded that the 48 000-Mr protein is the analogue to EF-TuE. coli, and that yeast mitochondrial EF-Tu is functionally and structurally more related to bacterial EF-Tu than cytosolic EF-1 of the same cell.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1983.tb07353.x/pdf
Ending Page	240
Page Count	6
Starting Page	235
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1983.tb07353.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	132
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1983-05-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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