Sequence homology between EF-1α, the α-chain of elongation factor 1 from Artemia salina and elongation factor EF-TU from Escherichia coli

In the course of a structural analysis of the α-chain of elongation factor 1 from Artemia salina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli...

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Bibliographic Details
Published in:FEBS letters 1983-03, Vol.153 (1), p.37-42
Main Authors: Amons, Reinout, Pluijms, Wim, Roobol, Kees, Möller, Wim
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Artemia - analysis
Biological Evolution
Escherichia coli - analysis
Eukaryotic elongation factor
Peptide Elongation Factor 1
Peptide Elongation Factor Tu
Peptide Elongation Factors
Peptide Fragments
Primary structure
Protein evolution
Sequence homology
Trypsin
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Summary:In the course of a structural analysis of the α-chain of elongation factor 1 from Artemia salina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli reveals a clear correspondence between the eukaryotic and prokaryotic protein throughout their polypeptide chains. The results support a basic conservation of the structure of the aminoacyl-tRNA carrying enzyme in evolution. The occurrence, in the eukaryotic factor, of several ϵ-trimethyllysine residues, is remarkable.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80115-X