The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins - PubMed (original) (raw)
. 2008 Feb 15;376(2):414-26.
doi: 10.1016/j.jmb.2007.10.088. Epub 2007 Nov 9.
Affiliations
- PMID: 18164725
- DOI: 10.1016/j.jmb.2007.10.088
The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins
Hélène Hodak et al. J Mol Biol. 2008.
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.
Similar articles
- Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussis.
Wohlkönig A, Hodak H, Clantin B, Sénéchal M, Bompard C, Jacob-Dubuisson F, Villeret V. Wohlkönig A, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Sep 1;64(Pt 9):809-12. doi: 10.1107/S1744309108024731. Epub 2008 Aug 9. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 18765910 Free PMC article. - Structure and plasticity of the peptidyl-prolyl isomerase Par27 of Bordetella pertussis revealed by X-ray diffraction and small-angle X-ray scattering.
Clantin B, Leyrat C, Wohlkönig A, Hodak H, Ribeiro Ede A Jr, Martinez N, Baud C, Smet-Nocca C, Villeret V, Jacob-Dubuisson F, Jamin M. Clantin B, et al. J Struct Biol. 2010 Mar;169(3):253-65. doi: 10.1016/j.jsb.2009.11.007. Epub 2009 Nov 20. J Struct Biol. 2010. PMID: 19932182 - The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
Behrens S, Maier R, de Cock H, Schmid FX, Gross CA. Behrens S, et al. EMBO J. 2001 Jan 15;20(1-2):285-94. doi: 10.1093/emboj/20.1.285. EMBO J. 2001. PMID: 11226178 Free PMC article. - Filamentous hemagglutinin of Bordetella pertussis: a key adhesin with immunomodulatory properties?
Villarino Romero R, Osicka R, Sebo P. Villarino Romero R, et al. Future Microbiol. 2014;9(12):1339-60. doi: 10.2217/fmb.14.77. Future Microbiol. 2014. PMID: 25517899 Review. - Multidomain Peptidyl Prolyl cis/trans Isomerases.
Schiene-Fischer C. Schiene-Fischer C. Biochim Biophys Acta. 2015 Oct;1850(10):2005-16. doi: 10.1016/j.bbagen.2014.11.012. Epub 2014 Nov 18. Biochim Biophys Acta. 2015. PMID: 25445709 Review.
Cited by
- BING, a novel antimicrobial peptide isolated from Japanese medaka plasma, targets bacterial envelope stress response by suppressing cpxR expression.
Dong M, Kwok SH, Humble JL, Liang Y, Tang SW, Tang KH, Tse MK, Lei JH, Ramalingam R, Koohi-Moghadam M, Au DWT, Sun H, Lam YW. Dong M, et al. Sci Rep. 2021 Jun 9;11(1):12219. doi: 10.1038/s41598-021-91765-4. Sci Rep. 2021. PMID: 34108601 Free PMC article. - Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.
Ünal CM, Steinert M. Ünal CM, et al. Microbiol Mol Biol Rev. 2014 Sep;78(3):544-71. doi: 10.1128/MMBR.00015-14. Microbiol Mol Biol Rev. 2014. PMID: 25184565 Free PMC article. Review. - Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
Jakob RP, Koch JR, Burmann BM, Schmidpeter PA, Hunkeler M, Hiller S, Schmid FX, Maier T. Jakob RP, et al. J Biol Chem. 2015 Feb 6;290(6):3278-92. doi: 10.1074/jbc.M114.622910. Epub 2014 Dec 17. J Biol Chem. 2015. PMID: 25525259 Free PMC article. - Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussis.
Wohlkönig A, Hodak H, Clantin B, Sénéchal M, Bompard C, Jacob-Dubuisson F, Villeret V. Wohlkönig A, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Sep 1;64(Pt 9):809-12. doi: 10.1107/S1744309108024731. Epub 2008 Aug 9. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 18765910 Free PMC article. - SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.
Figaj D, Ambroziak P, Rzepka I, Skórko-Glonek J. Figaj D, et al. Int J Mol Sci. 2022 Dec 24;24(1):295. doi: 10.3390/ijms24010295. Int J Mol Sci. 2022. PMID: 36613738 Free PMC article. Review.