Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu·aminoacyl-tRNA complex with temperature
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)01318-U/fullpdf
Reference14 articles.
1. How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
2. Impaired in vitro kinetics of EF-Tu mutant Aa
3. Hyper-accurate ribosomes inhibit growth.
4. Kinetic properties of Escherichia coli ribosomes with altered forms of S12
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1. Multiple stages in codon–anticodon recognition:double-trigger mechanisms and geometric constraints☆;Biochimie;2006-08
2. EF-Tu, a GTPase odyssey;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1998-11
3. Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli;Biochimica et Biophysica Acta (BBA) - General Subjects;1996-10
4. Elongation in bacterial protein biosynthesis;Current Opinion in Biotechnology;1996-08
5. Dissociation rates of peptidyl-tRNA from the P-site of E.coli ribosomes.;The EMBO Journal;1996-03
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