Prokaryotic Enhancer-Binding Proteins Reflect Eukaryote-Like Modularity: the Puzzle of Nitrogen Regulatory Protein C
This work was funded by NIH grant GM38361 to S.K.
Journal of bacteriology
Prokaryotes -- Genetics, Carrier proteins -- Analysis, Carrier proteins -- Structure, Prokaryotes -- Protein binding
Eukaryotic enhancer-binding proteins are often modular in design in that they are composed of physically separable domains that can function independently of one another (18, 46, 55). Detailed analyses have identified regions involved in specific DNA recognition and others involved in activation of transcription. In fact, in many instances, combining a domain from one protein with a second domain from another has produced a chimeric protein that demonstrates the expected functional properties of each parent (3, 19, 21, 22). As outlined below, members of a family of prokaryotic enhancer-binding proteins are also modular in structure. However, one member of the family, the NTRC protein (nitrogen regulatory protein C; also called NRI) of enteric bacteria, is apparently an exception. Comparison of the sequence of NTRC with that of other activators and with the sequence and structure of the factor for inversion stimulation (FIS) reveals a likely explanation for the puzzling properties of NTRC.
North, ANNE K., et al. "Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: the puzzle of nitrogen regulatory protein C." Journal of bacteriology 175.14 (1993): 4267.