Effect of Kirromycin on Elongation Factor Tu. Location of the Catalytic Center for Ribosome . Elongation-Factor-Tu GTPase Activity on the Elongation Factor
نویسندگان
چکیده
منابع مشابه
GTPase activation of elongation factor EF-Tu by the ribosome during decoding.
We have used single-particle reconstruction in cryo-electron microscopy to determine a structure of the Thermus thermophilus ribosome in which the ternary complex of elongation factor Tu (EF-Tu), tRNA and guanine nucleotide has been trapped on the ribosome using the antibiotic kirromycin. This represents the state in the decoding process just after codon recognition by tRNA and the resulting GT...
متن کاملGTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site.
Interaction of the elongation factor EF-Tu with the antibiotic kirromycin results in activation of the GTPase center of the factor and in induction of an additional tRNA binding site (tRNA binding site II to distinguish it from the classical tRNA binding site I). Activation of the GTPase center under these conditions is stimulated by addition of tRNA. Two-fold evidence is presented that this st...
متن کاملKirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu.
Kirromycin, a new inhibitor of protein synthesis, is shown to interfere with the peptide transfer reaction by acting on elongation factor Tu (EF-Tu). All the reactions associated with this elongation factor are affected. Formation of the EF-Tu.GTP complex is strongly stimulated. Peptide bond formation is prevented only when Phe-tRNA(Phe) is bound enzymatically to ribosomes, presumably because G...
متن کاملInteraction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts.
Elongation factor (EF) Tu promotes the binding of aminoacyl-tRNA (aa-tRNA) to the acceptor site of the ribosome. This process requires the formation of a ternary complex (EF-Tu.GTP.aa-tRNA). EF-Tu is released from the ribosome as an EF-Tu.GDP complex. Exchange of GDP for GTP is carried out through the formation of a complex with EF-Ts (EF-Tu.Ts). Mammalian mitochondrial EF-Tu (EF-Tu(mt)) differ...
متن کاملThe molecular basis of kirromycin (mocimycin) action; a 1H NMR study using deuterated elongation factor Tu.
The binding of the antibiotic kirromycin (mocimycin) to its target protein, bacterial elongation factor Tu (EF-Tu), has been studied by 1H NMR spectroscopy using deuterated protein. Narrow lines were observed in the spectrum of the unbound protein (due to residual protons) and in the spectrum of the kirromycin-EF-Tu complex. The spectrum of the complex has been compared with the spectra of the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11503.x