TY - JOUR
T1 - Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts
AU - Peter, Marcus E.
AU - Reiser, Christian O A
AU - Schirmer, Norbert K.
AU - Kiefhaber, Thomas
AU - Ott, Günther
AU - Grillenbeck, Norbert W.
AU - Sprinzl, Mathias
N1 - Funding Information:
This work was supported by the Deutsche Forschungs-gemeinschaft, SFB 213 D5, and by the Fonds der Chemischen Industrie.
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
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U2 - 10.1093/nar/18.23.6889
DO - 10.1093/nar/18.23.6889
M3 - Article
C2 - 2263451
AN - SCOPUS:0025612150
SN - 0305-1048
VL - 18
SP - 6889
EP - 6893
JO - Nucleic acids research
JF - Nucleic acids research
IS - 23
ER -