Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli.
The periplasmic fates of misfolded MalE31, a defective folding mutant of the maltose-binding protein, were determined by manipulating two cellular activities affecting the protein folding pathway in host cells: (i) the malEp promoter activity, which is controlled by the transcriptional activator MalT, and (ii) the DegP and Protease III periplasmic proteolytic activity. At a low level of expression, the degradation of misfolded MalE31 was partially impaired in cells lacking DegP or Protease III. At a high level of expression, misfolded MalE31 rapidly formed periplasmic inclusion bodies and thus escaped degradation. However, the manipulated host cell activities did not enhance the production of periplasmic, soluble MalE31. A kinetic competition between folding, aggregation, and degradation is proposed as a general model for the biogenesis of periplasmic proteins.[1]References
- Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli. Betton, J.M., Sassoon, N., Hofnung, M., Laurent, M. J. Biol. Chem. (1998) [Pubmed]
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