Biopolym. Cell. 1989; 5(1):80-83.
Short Communications
Initiation factor 3 (IF-3) of Escherichia coli is a substrate for Leu(Phe)-tRNA-protein transferase
- A. N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR
Moscow, USSR
Abstract
Initiation factor 3 (IF-3) of Escherichia coli is a substrate for Leu(Phe)-tRNA-protehl transferase (EC 2.3.2.6). Of the two polypeptide chains, only the short one (β or s) can be modified by the attachment of leucine, phenylalanine or methionine to the N-terminal amino acid residue of the chain.
Full text: (PDF, in Russian)
References
[1]
Grunberg-Manago M, Gros F. Initiation mechanisms of protein syntehesis. Prog Nucleic Acid Res Mol Biol. 1977;20:209-84.
[2]
Lee-Huang S, Ochoa S. Purification and properties of two messenger-discriminating species of E. coli initiation factor 3. Arch Biochem Biophys. 1973;156(1):84-96.
[3]
Suryanarayana T, Subramanian AR. Separation of two forms of IF-3 in Escherichia coli by two-dimensional gel electrophoresis. FEBS Lett. 1977;79(2):264-8.
[4]
Brauer D, Wittmann-Liebold B. The primary structure of the initiation factor IF-3 from Escherichia coli. FEBS Lett. 1977;79(2):269-75.
[5]
Leibowitz MJ, Soffer RL. Enzymatic modification of proteins. VII. Substrate specificity of leucyl,phenylalanyl-transfer ribonucleic acid-protein transferase. J Biol Chem. 1971;246(17):5207-12.
[6]
Soffer RL. Post-translational modification of proteins catalyzed by aminoacyl-tRNA-protein transferases. Mol Cell Biochem. 1973;2(1):3-14.
[7]
Gavrilova LP, Smolyaninov VV. Study of the mechanism of translocation in ribosomes. 1. Polyphenylalanine synthesis in Escherichia coli ribosomes without participation of guanosine-5'-triphosphate and protein translation factors. Mol Biol. 1971;5(6):710-7.
[8]
Hershey JW, Yanov J, Johnston K, Fakunding JL. Purification and characterization of protein synthesis initiation factors IF1, IF2, and IF3 from Escherichia coli. Arch Biochem Biophys. 1977;182(2):626-38.
[9]
Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[10]
Bachmair A, Finley D, Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 1986;234(4773):179-86.