title: The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins.
abstract: Proteins that pass through the periplasm in an unfolded state are highly sensitive to proteolysis and aggregation and, therefore, often require protection by chaperone-like proteins. The periplasm of Gram-negative bacteria is well equipped with ATP-independent chaperones and folding catalysts, including peptidyl-prolyl isomerases (PPIases). The filamentous hemagglutinin of Bordetella pertussis, which is secreted by the two-partner secretion pathway, crosses the periplasm in an unfolded conformation. By affinity chromatography, we identified a new periplasmic PPIase of the parvulin family, Par27, which binds to an unfolded filamentous hemagglutinin fragment. Par27 differs from previously characterized bacterial and eukaryotic parvulins. Its central parvulin-like domain is flanked by atypical N- and C-terminal extensions that are found in a number of putative PPIases present mostly in beta proteobacteria. Par27 displays both PPIase and chaperone activities in vitro. In vivo, Par27 might function as a general periplasmic chaperone in B. pertussis.
authors.affiliation: INSERM U629, Lille, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Hodak
authors.forename: Alexandre
authors.initials: A
authors.lastname: Wohlkönig
authors.forename: Caroline
authors.initials: C
authors.lastname: Smet-Nocca
authors.forename: Hervé
authors.initials: H
authors.lastname: Drobecq
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Wieruszeski
authors.forename: Magalie
authors.initials: M
authors.lastname: Sénéchal
authors.forename: Isabelle
authors.initials: I
authors.lastname: Landrieu
authors.forename: Camille
authors.initials: C
authors.lastname: Locht
authors.forename: Marc
authors.initials: M
authors.lastname: Jamin
authors.forename: Françoise
authors.initials: F
authors.lastname: Jacob-Dubuisson
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001886:Bordetella pertussis / Q000201:enzymology* / Q000235:genetics*; D018832:Molecular Chaperones / Q000378:metabolism*; D008970:Molecular Weight; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D019897:Periplasm / Q000201:enzymology; D010957:Plasmids; D017434:Protein Structure, Tertiary; D010566:Virulence Factors, Bordetella / Q000737:chemistry / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D018832:Molecular Chaperones; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D010566:Virulence Factors, Bordetella; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; D019696:Peptidylprolyl Isomerase