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The primary structure of elongation factor EF‐1 alpha from the brine shrimp Artemia.
Author(s) -
Hemert F.J.,
Amons R.,
Pluijms W.J.,
Ormondt H.,
Möller W.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01937.x
Subject(s) - biology , brine shrimp , shrimp , elongation factor , artemia salina , eukaryotic translation elongation factor 1 alpha 1 , fishery , biochemistry , medicine , gene , ribosome , rna , toxicity
cDNA as well as amino acid sequencing has revealed the complete primary structure of elongation factor EF‐1 alpha from the brine shrimp Artemia. A comparison with the published sequences of bacterial EF‐Tu, mitochondrial EF‐Tu and chloroplastic EF‐Tu shows that distinct areas of these polypeptide chains are conserved in evolution. The evolutionary distance between prokaryotic and eukaryotic types of EF‐Tu is larger than among bacterial and organellar EF‐ Tus . A number of regions present in both EF‐Tu and EF‐G from Escherichia coli are also found in EF‐1 alpha from Artemia.