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SecB--a chaperone dedicated to protein translocation
Article de revue   Avec comité de lecture

SecB--a chaperone dedicated to protein translocation

Philipp Bechtluft, Nico Nouwen, Sander J Tans et Arnold J M Driessen
Molecular bioSystems, Vol.6(4), pp.620-627
01/01/2010
PMID: 20237639

Résumé

Bacterial Proteins - chemistry Bacterial Proteins - metabolism Gram-Negative Bacteria - metabolism Models, Biological Models, Molecular Molecular Chaperones - chemistry Molecular Chaperones - metabolism Protein Folding Protein Processing, Post-Translational Protein Transport Systems Biology
SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

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