AbstractA short form of Escherichia coli translational initiation factor IF3, repeatedly found both in vivo and in vitro, lacking the positively charged N-terminal hexapeptide has been produced by mild trypsinization. The properties of this short form of IF3 have been studied. Compared to the long native form of the factor, the shortened IF3 displays a markedly decreased thermal stability and affinity for the 30 S ribosomal sub-unit, as well as a reduced biological activity in protein synthesis. Following the loss of the N-terminal hexapeptide, a second peptide bond (Lys-90Val-91) becomes easily accessible to proteolytic attack suggesting that formation of the short IF3 may be the first step in the physiological degradation of the factor
AbstractWe have studied the interactions between the ribosome and the domains of Escherichia coli tr...
Bacteria require three initiation factors, IF1, IF2 and IF3, to start protein synthesis. In the last...
AbstractInitiation factor IF2 from either Escherichia coli or Bacillus stearothermophilus was found ...
AbstractA short form of Escherichia coli translational initiation factor IF3, repeatedly found both ...
Starting from a synthetic modular gene (infA) encoding Escherichia coli translation initiation facto...
Initiation factor 3 (IF3) is one of the three conserved prokaryotic translation initiation factors e...
IF3C is the C-terminal domain of Escherichia coli translation initiation factor 3 (IF3) and is respo...
The functional properties of the two natural forms of Escherichia coli translation initiation factor...
During translation, initiation factor (IF) 3 binds to the small, 30S, ribosomal subunit and regulate...
Translation initiation factor IF2 is a guanine nucleotide-binding protein. The free energy change as...
Translation initiation factor IF3 is an essential bacterial protein, consisting of two domains (IF3C...
Initiation factor IF3 contains two domains separated by a flexible linker. While the isolated N-doma...
By means of limited proteolysis of Bacillus stearothermophilus initiation factor IF2 and genetic man...
AbstractWe have studied the interactions between the ribosome and the domains of Escherichia coli tr...
Bacteria require three initiation factors, IF1, IF2 and IF3, to start protein synthesis. In the last...
AbstractInitiation factor IF2 from either Escherichia coli or Bacillus stearothermophilus was found ...
AbstractA short form of Escherichia coli translational initiation factor IF3, repeatedly found both ...
Starting from a synthetic modular gene (infA) encoding Escherichia coli translation initiation facto...
Initiation factor 3 (IF3) is one of the three conserved prokaryotic translation initiation factors e...
IF3C is the C-terminal domain of Escherichia coli translation initiation factor 3 (IF3) and is respo...
The functional properties of the two natural forms of Escherichia coli translation initiation factor...
During translation, initiation factor (IF) 3 binds to the small, 30S, ribosomal subunit and regulate...
Translation initiation factor IF2 is a guanine nucleotide-binding protein. The free energy change as...
Translation initiation factor IF3 is an essential bacterial protein, consisting of two domains (IF3C...
Initiation factor IF3 contains two domains separated by a flexible linker. While the isolated N-doma...
By means of limited proteolysis of Bacillus stearothermophilus initiation factor IF2 and genetic man...
AbstractWe have studied the interactions between the ribosome and the domains of Escherichia coli tr...
Bacteria require three initiation factors, IF1, IF2 and IF3, to start protein synthesis. In the last...
AbstractInitiation factor IF2 from either Escherichia coli or Bacillus stearothermophilus was found ...