Jean‐François Collet

ORCID: 0000-0001-8069-7036
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About
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Research Areas
  • Bacterial Genetics and Biotechnology
  • Endoplasmic Reticulum Stress and Disease
  • Enzyme Structure and Function
  • Redox biology and oxidative stress
  • RNA and protein synthesis mechanisms
  • Genomics and Phylogenetic Studies
  • Protein Structure and Dynamics
  • Antibiotic Resistance in Bacteria
  • Bacteriophages and microbial interactions
  • Heat shock proteins research
  • Trace Elements in Health
  • Amino Acid Enzymes and Metabolism
  • Bacterial biofilms and quorum sensing
  • Metalloenzymes and iron-sulfur proteins
  • CAR-T cell therapy research
  • Monoclonal and Polyclonal Antibodies Research
  • Metabolism and Genetic Disorders
  • Biochemical and Molecular Research
  • Vibrio bacteria research studies
  • ATP Synthase and ATPases Research
  • Heme Oxygenase-1 and Carbon Monoxide
  • Photosynthetic Processes and Mechanisms
  • Glycosylation and Glycoproteins Research
  • Escherichia coli research studies
  • Cellular transport and secretion

de Duve Institute
2016-2025

Walloon Excellence in Lifesciences and Biotechnology
2016-2025

UCLouvain
2016-2025

KU Leuven
1997-2014

Redox (Norway)
2013

University of Michigan
2002-2008

The University of Texas at Austin
2004

Université Côte d'Azur
2002

Ludwig Cancer Research
1999

Physiol (Belgium)
1997

Abstract We have identified and characterized 95 mutations that reduce or abolish dye filling of amphid phasmid neurons little effect on viability, fertility movement. Twenty-seven occurred spontaneously in strains with a high frequency transposon insertion. Sixty-eight were isolated after treatment EMS. All the result defects one more chemosensory responses, such as chemotaxis to ammonium chloride formation dauer larvae under conditions starvation overcrowding. Seventy-five are alleles 12...

10.1093/genetics/139.1.171 article EN Genetics 1995-01-01

We report the sequence of a human cDNA that encodes 46 kDa transmembrane protein homologous to bacterial transporters for phosphate esters. This presents at its carboxy terminus consensus motif retention in endoplasmic reticulum. Northern blots rat tissues indicate corresponding mRNA is mostly expressed liver and kidney. In two patients with glycogen storage disease type Ib, mutations were observed either replaced conserved Gly Cys or introduced premature stop codon. The encoded therefore...

10.1016/s0014-5793(97)01463-4 article EN FEBS Letters 1997-12-15

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 in the bacterial periplasm. DsbG, thioredoxin-related protein, appears to be key player is first reductase identified periplasm Escherichia coli . Together with DsbC, DsbG controls global sulfenic acid content this compartment. Sulfenic formation...

10.1126/science.1179557 article EN Science 2009-11-20

Abstract Little is known on how β‐barrel proteins are assembled in the outer membrane (OM) of Gram‐negative bacteria. SurA has been proposed to be primary chaperone escorting bulk mass OM across periplasm. However, impact deletion global proteome not determined, limiting therefore our understanding function SurA. By using a differential proteomics approach based 2‐D LC‐MS n , we compared relative abundance 64 proteins, including 23 wild‐type and surA strains. Unexpectedly, found that loss...

10.1002/pmic.200800794 article EN PROTEOMICS 2009-04-02

Methylation of histone H3 on lysine 9 or 27 is crucial for heterochromatin formation. Previously considered hallmarks of, respectively, constitutive and facultative heterochromatin, recent evidence has accumulated in favor coexistence these two marks their cooperation gene silencing maintenance. H3K9me2/3 ensures anchorage at chromatin protein 1α (HP1α), a main component heterochromatin. HP1α chromoshadow domain, involved dimerization interaction with partners, additional but still unclear...

10.1128/mcb.00205-14 article EN Molecular and Cellular Biology 2014-07-22

Abstract The mechanical properties of the cell envelope in Gram-negative bacteria are controlled by peptidoglycan, outer membrane, and proteins interacting with both layers. In Escherichia coli , lipoprotein Lpp provides only covalent crosslink between membrane peptidoglycan. Here, we use single-cell atomic force microscopy genetically engineered strains to study contribution mechanics. We show that contributes stiffness two ways: covalently connecting controlling width periplasmic space....

10.1038/s41467-020-15489-1 article EN cc-by Nature Communications 2020-04-14

The cell envelope of gram-negative bacteria, a structure comprising an outer (OM) and inner (IM) membrane, is essential for life. OM the IM are separated by periplasm, compartment that contains peptidoglycan. tethered to peptidoglycan via lipoprotein, Lpp. However, importance envelope's multilayered architecture remains unknown. Here, when we removed physical coupling between peptidoglycan, cells lost ability sense defects in integrity. Further experiments revealed critical parameter...

10.1371/journal.pbio.2004303 article EN cc-by PLoS Biology 2017-12-19

The discovery of Escherichia coli Lpp as the first protein with three acyl groups covalently attached to its N-terminal cysteine residue defined a new class bacterial proteins, lipoproteins. Lipoproteins are extracytoplasmic, globular proteins that anchored membrane by lipid moiety. Being outer membrane, Lpp, which is also known Braun lipoprotein, small (5.8 kDa) and folds into trimeric helical structure. It numerically most abundant in E. coli. A unique feature C-terminal lysine...

10.1093/femsle/fny199 article EN FEMS Microbiology Letters 2018-08-10

ABSTRACT The envelope of Gram-negative bacteria is an essential compartment that constitutes a protective and permeability barrier between the cell its environment. also hosts wall, mesh-like structure made peptidoglycan (PG) determines shape provides osmotic protection. Since PG must grow divide in cell-cycle-synchronized manner, synthesis remodeling are tightly regulated. Here, we discovered homeostasis intimately linked to levels activation Cpx system, stress response system traditionally...

10.1128/mbio.00047-16 article EN cc-by mBio 2016-03-02

In Escherichia coli, the periplasmic disulfide oxidoreductase DsbA is thought to be a powerful but nonspecific oxidant, joining cysteines together moment they enter periplasm. DsbC, primary isomerase, likely resolves incorrect disulfides. Given reliance of protein function on correct bonds, it surprising that no phenotype has been established for null mutations in dsbC. Here we demonstrate entire DsbC isomerization pathway cause an increased sensitivity redox-active metal copper. We find...

10.1074/jbc.m505742200 article EN cc-by Journal of Biological Chemistry 2005-08-09
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