PMID:14691238
| Citation |
Laursen, BS, Kjaergaard, AC, Mortensen, KK, Hoffman, DW and Sperling-Petersen, HU (2004) The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker. Protein Sci. 13:230-9 |
|---|---|
| Abstract |
Bacterial translation initiation factor IF2 is a multidomain protein that is an essential component of a system for ensuring that protein synthesis begins at the correct codon within a messenger RNA. Full-length IF2 from Escherichia coli and seven fragments of the protein were expressed, purified, and characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) methods. Interestingly, resonances of the 6 kD IF2N domain located at the extreme N terminus of IF2 can be clearly identified within the NMR spectra of the full-length 97-kD protein. (15)N NMR relaxation rate data indicate that (1) the IF2N domain is internally well ordered and tumbles in solution in a manner that is independent of the other domains of the IF2 protein, and (2) the IF2N domain is connected to the C-terminal regions of IF2 by a flexible linker. Chemical shifts of resonances within the isolated IF2N domain do not significantly differ from those of the corresponding residues within the context of the full-length 97-kD protein, indicating that IF2N is a structurally independent unit that does not strongly interact with other regions of IF2. CD and NMR data together provide evidence that Domains I-III of IF2 have unstructured and flexible regions as well as substantial helical content; CD data indicate that the helical content of these regions decreases significantly at temperatures above 35 degrees C. The features of structurally well-ordered N- and C-terminal domains connected by a flexible linker with significant helical content are reminiscent of another translation initiation factor, IF3. |
| Links |
PubMed PMC2286522 Online version:10.1110/ps.03337604 |
| Keywords |
Amino Acid Sequence; Circular Dichroism; Cloning, Molecular; Computer Simulation; Conserved Sequence; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Molecular Weight; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments/analysis; Peptide Fragments/chemistry; Prokaryotic Initiation Factor-2/chemistry; Prokaryotic Initiation Factor-2/genetics; Prokaryotic Initiation Factor-2/isolation & purification; Prokaryotic Initiation Factor-2/metabolism; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Solutions/chemistry; Temperature |
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