Olivera Francetić

ORCID: 0000-0002-4145-5314
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • Escherichia coli research studies
  • RNA and protein synthesis mechanisms
  • Lipid Membrane Structure and Behavior
  • Bacterial biofilms and quorum sensing
  • Genomics and Phylogenetic Studies
  • Biochemical and Structural Characterization
  • Antibiotic Resistance in Bacteria
  • Transgenic Plants and Applications
  • Enzyme Production and Characterization
  • Vibrio bacteria research studies
  • Legume Nitrogen Fixing Symbiosis
  • Protein Structure and Dynamics
  • Toxin Mechanisms and Immunotoxins
  • Photosynthetic Processes and Mechanisms
  • Protist diversity and phylogeny
  • Heat shock proteins research
  • Chemical Synthesis and Analysis
  • Protein purification and stability
  • Viral gastroenteritis research and epidemiology
  • Cancer Research and Treatments
  • ATP Synthase and ATPases Research
  • Monoclonal and Polyclonal Antibodies Research
  • Supramolecular Self-Assembly in Materials

Institut Pasteur
2013-2023

Centre National de la Recherche Scientifique
2013-2023

Université Paris Cité
2022-2023

Laboratoire des Systèmes Macromoléculaires et Signalisation
2017

Centre de Gestion Scientifique
2017

Centre National pour la Recherche Scientifique et Technique (CNRST)
2010

Institute of Molecular Genetics
1993-1999

Tufts University
1993-1996

Enterohemorrhagic Escherichia coli (EHEC) O157:H7 causes hemorrhagic colitis and hemolytic uremic syndrome (HUS) by colonizing the gut mucosa producing Shiga toxins (Stx). The only factor clearly demonstrated to play a role in EHEC adherence intestinal epithelial cells is intimin, which binds host cell integrins nucleolin, as well receptor (Tir) that it injects into cell. Here we report produces adhesive type IV pili, term pilus (HCP), composed of 19-kDa pilin subunit (HcpA) encoded hcpA...

10.1172/jci30727 article EN Journal of Clinical Investigation 2007-10-19

More immediately, a strategy to inhibit the dysregulation of nNOS activity in skeletal muscle may be beneficial.

10.1172/jci30727c1 article EN Journal of Clinical Investigation 2008-02-01

Uropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides structural scaffold for displaying tip adhesin, FimH. We solved 4.2 Å resolution structure rod using cryo-electron microscopy. Residues forming interactive surfaces that determine mechanical properties were maintained by selection based on global alignment fimA...

10.7554/elife.31662 article EN cc-by eLife 2018-01-18

Chaperone proteins bind to newly synthesized polypeptides and assist in various assembly reactions. The Escherichia coli chaperone protein SecB binds precursors of exported assists export. In vitro, can many unfolded proteins. this report, we demonstrate that binding vivo is highly selective; the major are bound by nascent maltose-binding (MBP), LamB, OmpF, OmpA. These results support hypothesis primary physiological function stimulate By interacting with polypeptides, probably stimulates...

10.1128/jb.175.8.2184-2188.1993 article EN Journal of Bacteriology 1993-04-01

Many Gram-negative bacteria secrete specific proteins via the type II secretion systems (T2SS). These complex machineries share with related archaeal flagella and IV pilus (T4P) biogenesis ability to assemble thin, flexible filaments composed of small, initially inner membrane-localized called “pilins.” In T2SS from Klebsiella oxytoca , periplasmic pseudopili that are essential for pullulanase (PulA) extend beyond bacterial surface form pili when major pilin PulG is overproduced. Here, we...

10.1073/pnas.1001703107 article EN Proceedings of the National Academy of Sciences 2010-07-02

Systematic sequencing of the Escherichia coli K-12 chromosome (GenBank entry U18997) has revealed presence an apparently complete operon genes (the gspC-0 operon) similar to coding for components main terminal branch general secretory pathway (e.g., Klebsiella oxytoca pulC-0 pullulanase secretion and related required type IV pilus biogenesis. For example, last gene in gsp operon, gspO (formerly hopD), encodes a protein which is several prepilin peptidases. Expression from lacZp promotes...

10.1128/jb.178.12.3544-3549.1996 article EN cc-by Journal of Bacteriology 1996-06-01

The pseudopilin PulG is an essential component of the pullulanase-specific type II secretion system from Klebsiella oxytoca. major subunit a short, thin-filament pseudopilus, which presumably elongates and retracts in periplasm, acting as dynamic piston to promote pullulanase secretion. It has signal sequence-like N-terminal segment that, according studies with green red fluorescent protein chimeras, anchors unassembled inner membrane. We analyzed early steps membrane targeting insertion...

10.1128/jb.01230-06 article EN Journal of Bacteriology 2006-12-09

Summary In G ram‐negative bacteria, type IV pilus assembly ( T4PS ) and II secretion T2SS systems polymerize inner membrane proteins called major pilins or pseudopilins respectively, into thin filaments. Four minor are required in both for efficient fibre assembly. E scherichia coli K ‐12 has a set of genes that silent under standard growth conditions. We studied the heterologous . pilin PpdD by lebsiella oxytoca P ul system. this context depended on expression pseudopilin pulHIJK ppdAB ‐...

10.1111/mmi.12033 article EN Molecular Microbiology 2012-09-25

Type II secretion systems (T2SSs) promote of folded proteins playing important roles in nutrient acquisition, adaptation and virulence Gram-negative bacteria. Protein is associated with the assembly type 4 pilus (T4P)-like fibres called pseudopili. Initially membrane embedded, pseudopilin T4 pilin subunits share conserved transmembrane segments containing an invariant Glu residue at fifth position, E5. Mutations E5 major pilins PulG, Klebsiella T2SS abolish fibre function. Among four minor...

10.1111/mmi.13432 article EN Molecular Microbiology 2016-06-04

Abstract The type 2 secretion system (T2SS) is present in some Gram-negative eubacteria and used to secrete proteins across the outer membrane. Here we report that certain representative heteroloboseans, jakobids, malawimonads hemimastigotes unexpectedly possess homologues of core T2SS components. We show at least them are mitochondria, their behaviour biochemical assays consistent with presence a mitochondrial T2SS-derived (miT2SS). additionally identified 23 protein families co-occurring...

10.1038/s41467-021-23046-7 article EN cc-by Nature Communications 2021-05-19

Pullulanase (PulA) from the gram-negative bacterium Klebsiella oxytoca is a 116-kDa surface-anchored lipoprotein of isoamylase family that allows growth on branched maltodextrin polymers. PulA specifically secreted via type II secretion system. PelBsp-PulA, nonacylated variant made by replacing signal peptide (sp) with pectate lyase PelB Erwinia chrysanthemi, was efficiently into medium. Two 80-amino-acid regions PulA, designated A and B, were previously shown to promote beta-lactamase...

10.1128/jb.187.20.7045-7055.2005 article EN Journal of Bacteriology 2005-09-30

Abstract Background All aerobically grown living cells are exposed to oxidative damage by reactive oxygen species (ROS). A major ROS proteins is caused covalent modifications of methionine residues giving sulfoxide (Met-SO). Methionine reductases enzymes able regenerate and restore protein function after damage. Results We characterized the reductase genes msrA msrB in Bacillus subtilis , forming an operon transcribed from a single sigma A-dependent promoter. The msrAB was specifically...

10.1186/1471-2180-8-128 article EN cc-by BMC Microbiology 2008-07-28
Coming Soon ...