Tanja Florin

ORCID: 0000-0002-0176-6898
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About
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Research Areas
  • RNA and protein synthesis mechanisms
  • Antimicrobial Peptides and Activities
  • Bacterial Genetics and Biotechnology
  • RNA modifications and cancer
  • Bacteriophages and microbial interactions
  • Biochemical and Structural Characterization
  • Probiotics and Fermented Foods
  • Gut microbiota and health
  • Plant Parasitism and Resistance
  • Gastrointestinal motility and disorders
  • Fungal Biology and Applications
  • Clostridium difficile and Clostridium perfringens research
  • Inflammatory Bowel Disease
  • Diet and metabolism studies
  • Chemical synthesis and alkaloids
  • Microbial Natural Products and Biosynthesis
  • Chemical Synthesis and Analysis
  • Muscle metabolism and nutrition
  • Genomics and Phylogenetic Studies
  • Antibiotic Resistance in Bacteria
  • Toxin Mechanisms and Immunotoxins

University of Illinois Chicago
2014-2021

Ashland (United States)
2015

University of Potsdam
2014

Significance Macrolide antibiotics inhibit translation by binding in the ribosomal nascent peptide exit tunnel. It was believed that macrolides interfere with protein synthesis obstructing egress of proteins. In contrast to this view, results ribosome profiling analysis suggest main mode macrolide action is context-specific inhibition bond formation. The a molecule bound tunnel impaired catalysis formation between specific combinations peptidyl donors and aminoacyl acceptors, leading...

10.1073/pnas.1417334111 article EN Proceedings of the National Academy of Sciences 2014-10-27

With bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become promising area of focus in antibiotic research. AMPs are derived from diverse range species, prokaryotes humans, with mechanism action that often involves disruption the cell membrane. Proline-rich (PrAMPs) instead actively transported inside where they bind and inactivate specific targets. Recently, it was reported some PrAMPs, such as Bac71–35, oncocins apidaecins,...

10.1093/nar/gkw018 article EN cc-by-nc Nucleic Acids Research 2016-01-24

Biochemical studies suggested that the antimicrobial peptide apidaecin (Api) inhibits protein synthesis by binding in nascent exit tunnel and trapping release factor associated with a terminating ribosome. The mode of Api action bacterial cells had remained unknown. Here genome-wide analysis reveals bacteria, arrests translating ribosomes at stop codons causes pronounced queuing trailing ribosomes. By sequestering available factors, promotes pervasive codon bypass, leading to expression...

10.7554/elife.62655 article EN cc-by eLife 2020-10-08

Significance Apidaecin (Api) is a ribosome-targeting proline-rich antimicrobial peptide with unique mechanism of action. Api’s activity against Gram-negative pathogens makes it an attractive candidate for developing new antibiotics. The approaches based on analyzing the antibacterial chemically synthesized peptides fail to distinguish effects upon cellular uptake from those affecting on-target activity. By expressing comprehensive library api gene mutants in bacterial cell and composition by...

10.1073/pnas.2026465118 article EN Proceedings of the National Academy of Sciences 2021-03-05

OBJECTIVE: This study ascertains the relative contributions of genetics and environment in determining methane emission humans rats. There is considerable interest factors microbial species that inhabit colon. Methanogens, which are archaebacteria, an easily detected colonic luminal bacteria because they respire methane. They present some but not all human colons lower animal hindguts. Opinion varies on nature influencing this ecology with studies proposing existence host genetic influences....

10.1016/s0002-9270(00)01111-4 article EN The American Journal of Gastroenterology 2000-10-01

Abstract Biochemical studies suggested that the antimicrobial peptide apidaecin (Api) inhibits protein synthesis by binding in nascent exit tunnel and trapping release factor associated with a terminating ribosome. The mode of Api action bacterial cells had remained unknown. Here, genome-wide analysis revealed arrests translating ribosomes at stop codons causes pronounced queuing trailing ribosomes. By sequestering available factors, promotes pervasive codon bypass, leading to expression...

10.1101/2020.05.17.100735 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-05-20

Apidaecin (Api) belongs to the group of proline‐rich antimicrobial peptides (PrAMPs), which are produced by insects and mammals protect host from bacterial infection. PrAMPs enter cell, bind ribosome, inhibit protein synthesis. Biochemical characterization recent high‐resolution crystal structures have shown that most obstruct nascent peptide exit tunnel peptidyl transferase center in ribosome block initiation step translation. Despite lack structural information about Api‐bound its...

10.1096/fasebj.31.1_supplement.600.5 article EN The FASEB Journal 2017-04-01
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