A5002701361- Advanced biosensing and bioanalysis techniques
- Biosensors and Analytical Detection
- Redox biology and oxidative stress
- Endoplasmic Reticulum Stress and Disease
- Metalloenzymes and iron-sulfur proteins
- Sulfur Compounds in Biology
- Glutathione Transferases and Polymorphisms
- Bacterial Genetics and Biotechnology
- RNA and protein synthesis mechanisms
- Microfluidic and Bio-sensing Technologies
- Enzyme Structure and Function
- Peptidase Inhibition and Analysis
- Marine and coastal ecosystems
- bioluminescence and chemiluminescence research
- Vibrio bacteria research studies
- Bacterial Infections and Vaccines
- RNA Interference and Gene Delivery
- Molecular Biology Techniques and Applications
- Trace Elements in Health
- Nanofabrication and Lithography Techniques
- Microbial Metabolic Engineering and Bioproduction
- DNA and Nucleic Acid Chemistry
- Fungal and yeast genetics research
- Marine Toxins and Detection Methods
- Advanced Biosensing Techniques and Applications
Universitat Rovira i Virgili
2015-2022
The University of Texas at Austin
2003-2009
University of Michigan
2004
When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or monomeric apoprotein solution. Analytical and spectroscopic studies of wild-type protein site-directed variants structural characterization the by using x-ray crystallography indicate that contains subunit-bridging [2Fe-2S] cluster is ligated catalytic cysteines two glutaredoxins glutathiones. Mutagenesis data on variety suggest incorporation an...
We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is monomeric reductase, into [2Fe-2S] bridged dimer capable catalyzing O2-dependent sulfhydryl oxidation in vitro. Expression mutant protein Escherichia coli with oxidizing cytoplasm and secretion via Tat restored bond strains lacked complete periplasmic oxidative machinery (DsbA DsbB). The evolution thioredoxin illustrates how within an...
Organisms have evolved elaborate systems that ensure the homeostasis of thiol redox environment in their intracellular compartments. In Escherichia coli, cytoplasm is kept under reducing conditions by thioredoxins with help thioredoxin reductase and glutaredoxins small molecule glutathione reductase. As a result, disulfide bonds are constantly resolved this compartment. contrast to cytoplasm, periplasm E. coli maintained an oxidized state DsbA, which recycled DsbB. Thioredoxin 1, when...
Thioredoxin exported into the Escherichia coli periplasm catalyzes oxidation of protein thiols in a DsbB-dependent function. However, oxidative activity periplasmic thioredoxin is insufficient to render dsbA(-) cells susceptible infection by M13, phenotype that critically dependent on disulfide bond formation cell envelope. We sought examine molecular determinants are required order convert from reductant an efficient oxidant. A genetic screen for mutations sensitive M13 led isolation single...
The proliferation of harmful microalgae endangers aquatic ecosystems and can have serious economic implications on a global level. Harmful their associated toxins also pose threat to human health since they cause seafood-borne diseases such as ciguatera. Implementation DNA-based molecular methods together with appropriate detection strategies in monitoring programs support the efforts for effective prevention potential outbreaks. A PCR-lateral flow assay (PCR-LFA) dipstick format was...
Magnetic separation has been widely exploited for capture and detection of nucleic acids, including amplicons. Streptavidin-magnetic beads (SA-MB) are typically employed this purpose, as well in biosensing applications. However, remaining biotinylated primer the amplification reaction can compete with labeled amplicon binding to beads. Also, harsh conditions needed elution bound amplicons restrict their use purification purposes. Herein we show that a sequence-specific DNA protein...