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. 1990 Dec 11;18(23):6889–6893. doi: 10.1093/nar/18.23.6889

Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.

M E Peter 1, C O Reiser 1, N K Schirmer 1, T Kiefhaber 1, G Ott 1, N W Grillenbeck 1, M Sprinzl 1
PMCID: PMC332746  PMID: 2263451

Abstract

The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichroism spectroscopy, the isolated domain II/III does not contain any alpha-helical structure. Nucleotide exchange factor, EF-Ts, was found to interact with domain II/III, whereas the binding of aminoacyl-tRNA, GDP and GTP to this EF-Tu fragment could not be detected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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