Title :

Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein

Author(s) :

Baud, Catherine [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Gutsche, Irina [Auteur]
Unit for Virus Host-Cell Interactions [Grenoble] [UVHCI]
Willery, Eve [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
de Paepe, Diane [Auteur]
Institut de pharmacologie et de biologie structurale [IPBS]
Drobecq, Hervé [Auteur]
Mécanismes de tumorigenèse et thérapies ciblées
Gilleron, Martine [Auteur]
Institut de pharmacologie et de biologie structurale [IPBS]
Locht, Camille [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Jamin, Marc [Auteur]
Unit for Virus Host-Cell Interactions [Grenoble] [UVHCI]
Jacob-Dubuisson, Françoise [Auteur correspondant]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]

Journal title :

Molecular Microbiology

Pages :

1625-1636

Publisher :

Wiley

Publication date :

2011-06

ISSN :

0950-382X

HAL domain(s) :

Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire

English abstract : [en]

The chaperone/protease DegP belongs to the HtrA superfamily and is involved in protein quality control in the periplasm of Gram‐negative bacteria. In Escherichia coli, typical substrates are unfolded or misfolded globular ...
Show more >The chaperone/protease DegP belongs to the HtrA superfamily and is involved in protein quality control in the periplasm of Gram‐negative bacteria. In Escherichia coli, typical substrates are unfolded or misfolded globular proteins that trigger the rearrangement of inactive DegP hexamers into substrate‐sequestering 12‐ or 24‐mers ‘cages’ for refolding or degradation. In Bordetella pertussis, DegPBp facilitates, in addition, the secretion of FHA, a long β‐helical adhesin that passes through the periplasm in an extended conformation. We show that DegPBp exists as soluble trimers and as a membrane‐associated form. Different substrates interact differently with the distinct forms of DegPBp, and membrane‐associated DegPBp has high affinity for non‐native FHA. Unlike more globular substrates, FHA does not efficiently mediate rearrangement of trimers into proteolytically active, short‐lived dodecamers. In contrast to these dodecamers, membrane‐associated DegPBp is not committed to substrate degradation, although it is proteolytically competent. In B. pertussis, membrane‐associated DegPBp thus represents a specific functional form serving as a holding chaperone for client proteins including FHA. If FHA secretion is impaired, membrane‐associated DegPBp participates in its degradation. This form of DegPBp is appropriate to handle substrates unsuitable to be sequestered in cages or non‐folded, secretory proteins that must not be degraded.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

ANR Project :

Etude de la modulation de l'infection grippale par les protéases et les antiprotéases de l'hôte

Collections :

• Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017

Source :

Harvested from HAL