FlgM gains structure in living cells.
Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that FlgM gains structure inside living Escherichia coli cells and under physiologically relevant conditions in vitro, i.e., in solutions containing high concentrations (>/=400 g/liter) of glucose, BSA, or ovalbumin. Structure formation represents solute-induced changes in the equilibrium between the structured and disordered forms of FlgM. The results provide insight into how the environment of intrinsically disordered proteins could dictate their structure and, in turn, emphasize the relevance of studying proteins in living cells and in vitro under physiologically realistic conditions.
Dedmon
Matthew M
MM
Departments of Chemistry, and Biochemistry and Biophysics, and Lineberger Cancer Research Center, University of North Carolina, Chapel Hill, NC 27599, USA.
Patel
Chetan N
CN
Young
Gregory B
GB
Pielak
Gary J
GJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D005947:Glucose / Q000378:metabolism / Q000494:pharmacology; D006859:Hydrogen / Q000494:pharmacology; D009682:Magnetic Resonance Spectroscopy; D010047:Ovalbumin / Q000494:pharmacology; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; C071266:FlgM protein, Bacteria; D012710:Serum Albumin, Bovine; D006859:Hydrogen; D010047:Ovalbumin; D005947:Glucose