Folding and aggregation of export-defective mutants of the maltose-binding protein.

Res Microbiol

Unité de Repliement et de Modélisation des Protéines, Institut Pasteur, CNRS-URA 2185, Paris, France.

Published: September 2002

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.

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http://dx.doi.org/10.1016/s0923-2508(02)01338-4DOI Listing

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