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Folding and aggregation of export-defective mutants of the maltose-binding protein
Jean-Michel Betton1, Denis Phichith, Sabine Hunke
1Unité de Repliement et de Modélisation des Protéines, Institut Pasteur, CNRS-URA 2185, Paris, France. jmbetton@pasteur.fr
Research in Microbiology
|October 31, 2002
Abstract:
We previously characterized a defective-folding variant of the periplasmic maltose-binding protein, MalE31. To examine the alternative folding pathways open to the MalE31 precursor, we have analyzed the cellular fates of this aggregation-prone protein carrying altered signal sequences. Our results are most easily interpreted by a kinetic competition between exportation, folding, and degradation.