Folding mechanisms of periplasmic proteins

Autor: Jean-François Collet, Katleen Denoncin, Camille V. Goemans

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843:1517-1528

More than one fifth of the proteins encoded by the genome of Escherichia coli are destined to the bacterial cell envelope. Over the past 20years, the mechanisms by which envelope proteins reach their three-dimensional structure have been intensively

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ac4e132314d368e5042dcf6e81a503c
https://doi.org/10.1016/j.bbamcr.2013.10.014

A new role for Escherichia coli DsbC protein in protection against oxidative stress

Autor: Isabelle S. Arts, Didier Vertommen, Joris Messens, Sophie Rahuel-Clermont, Camille V. Goemans, Katleen Denoncin, Jean-François Collet

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (18), pp.12356-12364. ⟨10.1074/jbc.M114.554055⟩

International audience; Background: DsbC is a protein-disulfide isomerase present in the periplasm of Gram-negative bacteria. Results: We discovered that DsbC also regulates the redox state of the single cysteine residue of the l-arabinose-binding pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff76e290482f245e3cc8231befd176fc
https://doi.org/10.1074/jbc.m114.554055

Protein disulfide bond formation in the periplasm: determination of the in vivo redox state of cysteine residues

Autor: Valérie Nicolaes, Katleen Denoncin, Pauline Leverrier, Seung-Hyun Cho, Jean-François Collet

Publikováno v: Methods in Molecular Biology
Methods in Molecular Biology ISBN: 9781627032445

Many proteins secreted to the bacterial cell envelope contain cysteine residues that are involved in disulfide bonds. These disulfides either play a structural role, increasing protein stability, or reversibly form in the catalytic site of periplasmi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::136b8c03f7c75264228e8f4634fa8ed5

Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC*

Autor: Seung-Hyun Cho, Katleen Denoncin, Annie Hiniker, Pauline Leverrier, Jean-Paul Declercq, Jean-François Collet, Didier Vertommen

The bacterial Rcs phosphorelay is a stress-induced defense mechanism that controls the expression of numerous genes, including those for capsular polysaccharides, motility, and virulence factors. It is a complex multicomponent system that includes th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1501f7700d7f3176c842ff4ec9b94674
https://europepmc.org/articles/PMC3089515/

A periplasmic reducing system protects single cysteine residues from oxidation

Autor: Katleen Denoncin, Joris Messens, Pierre Morsomme, Jean-François Collet, Khadija Wahni, Kate S. Carroll, Didier Vertommen, Matthieu Depuydt, Stephen E. Leonard

Publikováno v: Science (New York, N.Y.). 326(5956)

Periplasmic Redox Regulation The oxidation state of intracellular and extracellular proteins are carefully managed by cellular redox machineries. Depuydt et al. (p. 1109 ) discovered a reducing system that protects single cysteine residues from oxida

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f510a56ef9c4e9ab6de6573cbd70dfd3
https://pubmed.ncbi.nlm.nih.gov/19965429