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• W1990122427 abstract "Elongation factor 1, a complex involved in protein biosynthesis, contains two guanine-nucleotide-exchange proteins EF-1 beta and EF-1 delta. The sequence of EF-1 delta of Artemia was determined with the purified protein. When compared to EF-1 delta from Xenopus, a high degree of identify (80%) was found in the C-terminal domains of the proteins, which contain the guanine-nucleotide-exchange activity. The N-terminal domains share only 23% of the amino acids at identical positions, and therefore they were further analysed for less obvious types of homology. To this end, a published approach for sequence analysis, which can detect peculiar amino acid patterns in proteins was applied. In this way, a weak albeit unmistakable similarity between the two EF-1 delta proteins was demonstrated in the region of the leucine-zippers, apart from the leucine repeat itself. Apparently, they display a common structural pattern in their N-terminal domains, which so far has been observed mainly in transcription factors." @default.
• W1990122427 created "2016-06-24" @default.
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• W1990122427 date "1994-08-01" @default.
• W1990122427 modified "2023-09-27" @default.
• W1990122427 title "The leucine-zipper in elongation factor EF-1δ, a guanine-nucleotide exchange protein, is conserved in Artemia and Xenopus" @default.
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• W1990122427 doi "https://doi.org/10.1016/0167-4781(94)90187-2" @default.
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