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Article

Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate.

The Journal of biological chemistry - 3 Oct 2003

Wolff Nicolas, Sapriel Guillaume, Bodenreider Christophe, Chaffotte Alain, Delepelaire Philippe

Abstract excerpt

We have previously shown that SecB, the ATP-independent chaperone of the Sec pathway, is required for the secretion of the HasA hemophore from Serratia marcescens via its type I secretion pathway, both in the reconstituted system in Escherichia coli and in the original host. The refolding of apo-HasA after denaturation with guanidine HCl was followed by stopped-flow measurements of fluorescence of its single...

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Identifiers

PMID: 12829711
DOI: 10.1074/jbc.M302322200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate.PMID 12829711Read ↗

Folded HasA inhibits its own secretion through its ABC exporter.Semantic proximity Read ↗

The N terminus of the HasA protein and the SecB chaperone cooperate in the efficient targeting and secretion of HasA via the ATP-binding cassette transporter.Semantic proximity Read ↗

Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate.Semantic proximity Read ↗

The heme transfer from the soluble HasA hemophore to its membrane-bound receptor HasR is driven by protein-protein interaction from a high to a lower affinity binding site.Semantic proximity Read ↗

Amino acid replacements in the Serratia marcescens haemolysin ShIA define sites involved in activation and secretion.Semantic proximity Read ↗

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.Semantic proximity Read ↗

Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.Semantic proximity Read ↗

A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli.Semantic proximity Read ↗

Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteins.Semantic proximity Read ↗

The rapid degradation of mutant SecA protein in the Bacillus subtilis secA341 (ts) mutant causes a protein translocation defect in the cell.Semantic proximity Read ↗

Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade.Semantic proximity Read ↗

Binding of HasA by its transmembrane receptor HasR follows a conformational funnel mechanism.Semantic proximity Read ↗

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