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

Marcus E. Peter, Christian O A Reiser, Norbert K. Schirmer, Thomas Kiefhaber, Günther Ott, Norbert W. Grillenbeck, Mathias Sprinzl*

*Corresponding author for this work

Research output: Contribution to journalArticle

24 Scopus citations

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 α-hellcal structure. Nucleotide exchange factor, EF-Ts, was found to Interact with domain II/III, whereas the binding of amlnoacyl-tRNA, GDP and GTP to this EF-Tu fragment could not be detected.

Original languageEnglish (US)
Pages (from-to)6889-6893
Number of pages5
JournalNucleic acids research
Volume18
Issue number23
DOIs
StatePublished - Dec 1 1990

ASJC Scopus subject areas

  • Genetics

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