Interaction of the isolated domain II/III ofThermus thermophiluselongation factor Tu with the nucleotide exchange factor EF-Ts | Zendy

Marcus E. Peter | Zendy; Christian O. A. Reiser | Zendy; Norbert K. Schirmer | Zendy; Thomas Kiefhaber | Zendy; Günther Ott | Zendy; Norbert Grillenbeck | Zendy; Mathias Sprinzl | Zendy

Open Access

Interaction of the isolated domain II/III ofThermus thermophiluselongation factor Tu with the nucleotide exchange factor EF-Ts

Author(s) -

Marcus E. Peter,

Christian O. A. Reiser,

Norbert K. Schirmer,

Thomas Kiefhaber,

Günther Ott,

Norbert Grillenbeck,

Mathias Sprinzl

Publication year - 1990

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/18.23.6889

Subject(s) - thermus thermophilus , biology , elongation factor , circular dichroism , thermus aquaticus , ef tu , cyclic nucleotide binding domain , nucleotide , gtp' , guanosine triphosphate , guanine nucleotide exchange factor , thermus , denaturation (fissile materials) , biochemistry , crystallography , biophysics , gtpase , escherichia coli , transfer rna , chemistry , ribosome , enzyme , thermophile , rna , nuclear chemistry , gene

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research