Although protein disulphide isomerase (PDI) has been known for nearly 40 years, several new PDIs have recently been described that reveal a remarkable diversity in both structure and function. This article reviews our current knowledge of the PDI family members and identifies four novel PDIs in the human genome. These include human transmembrane proteins that have C. elegans or Drosophila orthologues for which a developmental role has been proven. Their role in development, together with other functional roles for PDIs such as conferring resistance to apoptosis under hypoxia and a potential role in the oxygen-sensing apparatus are discussed.
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http://dx.doi.org/10.1002/bies.10287 | DOI Listing |
Redox Biol
November 2023
Department of Selenoprotein Research and the National Tumor Biology Laboratory, National Institute of Oncology, 1122, Budapest, Hungary; Division of Biochemistry, Department of Medical Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden. Electronic address:
TXNL1 (also named TRP32, for thioredoxin related protein of 32 kDa) is a cytosolic thioredoxin-fold protein expressed in all cell types and conserved from yeast to mammals, but with yet poorly known function. Here, we expressed and purified human TXNL1 together with several Cys-to-Ser variants, characterizing their enzymatic properties. TXNL1 could reduce disulfides in insulin, cystine and glutathione disulfide (GSSG) in reactions coupled to thioredoxin reductase (TXNRD1, TrxR1) using NADPH, similarly to thioredoxin (TXN, Trx1), but with lower catalytic efficacy due to at least one order of magnitude higher K of TrxR1 for TXNL1 compared to Trx1.
View Article and Find Full Text PDFMicrobiol Spectr
March 2023
Institut Pasteur, Université Paris Cité, CNRS UMR6047, Biology of Gram-Positive Pathogens Unit, Paris, France.
Streptococcus gallolyticus subsp. () is an opportunistic gut pathogen associated with colorectal cancer. We previously showed that colonization of the murine colon by in tumoral conditions was strongly enhanced by the production of gallocin A, a two-peptide bacteriocin.
View Article and Find Full Text PDFJ Genet Eng Biotechnol
July 2022
Molecular Biology Department, Biotechnology Research Institute, National Research Centre, 33 El Bohouth St., Dokki, P.O. Box: 12622, Giza, Egypt.
Background: The freshwater snails Biomphalaria alexandrina (Gastropoda: Planorbidae) has public health importance of being an intermediate host of Schistosoma mansoni, the parasite species that causes intestinal schistosomiasis in humans. Glutathione transferases (GSTs) play an important role in detoxification of a broad range of compounds including secondary metabolites and exogenous compounds. Studying GSTs in snails may clarify their role in detoxification of molluscicides.
View Article and Find Full Text PDFCurr Res Struct Biol
April 2022
Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, 35392, Giessen, Germany.
Plasmoredoxin is a 22 kDa thiol-disulfide oxidoreductase involved in cellular redox regulatory processes and antioxidant defense. The 1.6 Å structure of the protein, solved via X-ray crystallography, adopts a modified thioredoxin fold.
View Article and Find Full Text PDFBiophys J
March 2022
Institute for Biological and Medical Engineering, Schools of Engineering, Medicine and Biological Sciences, Pontificia Universidad Católica de Chile, Santiago, Chile; ANID - Millennium Science Initiative Program - Millennium Institute for Integrative Biology (iBio), Santiago, Chile. Electronic address:
Cyanobacteria possesses the simplest circadian clock, composed of three proteins that act as a phosphorylation oscillator: KaiA, KaiB, and KaiC. The timing of this oscillator is determined by the fold-switch of KaiB, a structural rearrangement of its C-terminal half that is accompanied by a change in the oligomerization state. During the day, KaiB forms a stable tetramer (gsKaiB), whereas it adopts a monomeric thioredoxin-like fold during the night (fsKaiB).
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