FlgM gains structure in living cells

AUTOR(ES)

Dedmon, Matthew M.

FONTE

The National Academy of Sciences

RESUMO

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.

Documentos Relacionados

• Flk Couples flgM Translation to Flagellar Ring Assembly in Salmonella typhimurium
• Role of FlgM in sigma D-dependent gene expression in Bacillus subtilis.
• The flagellar anti-σ factor FlgM actively dissociates Salmonella typhimurium σ28 RNA polymerase holoenzyme
• Mutation of flgM attenuates virulence of Salmonella typhimurium, and mutation of fliA represses the attenuated phenotype.
• The attenuated phenotype of a Salmonella typhimurium flgM mutant is related to expression of FliC flagellin.