The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665069 | PMC |
| http://dx.doi.org/10.1074/jbc.M809509200 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Unveiling the versatility of the thioredoxin framework: Insights from the structural examination of DsbA1.
Comput Struct Biotechnol J
December 2024
Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, School of Agriculture, Biomedicine and Environment, La Trobe University, Bundoora, Australia.
In bacteria the formation of disulphide bonds is facilitated by a family of enzymes known as the disulphide bond forming (Dsb) proteins, which, despite low sequence homology, belong to the thioredoxin (TRX) superfamily. Among these enzymes is the disulphide bond-forming protein A (DsbA); a periplasmic thiol oxidase responsible for catalysing the oxidative folding of numerous cell envelope and secreted proteins. Pathogenic bacteria often contain diverse Dsb proteins with distinct functionalities commonly associated with pathogenesis.
View Article and Find Full Text PDFCorrection: Muñoz-Villagrán et al. The Thioredoxin Fold Protein (TFP2) from Extreme Acidophilic sp. CF-1 Is a Chaperedoxin-like Protein That Prevents the Aggregation of Proteins under Oxidative Stress. 2024, , 6905.
Int J Mol Sci
November 2024
Laboratorio de Microbiología Básica y Aplicada, Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Santiago 9170022, Chile.
Susanne Sievers and Daniela Zühlke were not included as authors in the original publication [...
View Article and Find Full Text PDFThe serine protease DPP9 and the redox sensor KEAP1 form a mutually inhibitory complex.
J Biol Chem
November 2024
Pharmacology Program of the Weill Cornell Graduate School of Medical Sciences, Memorial Sloan Kettering Cancer Center, New York, New York, USA; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA; Tri-Institutional PhD Program in Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, New York, USA. Electronic address:
Synthetic inhibitors of the serine protease DPP9 activate the related NLRP1 and CARD8 inflammasomes and stimulate powerful innate immune responses. Thus, it seems plausible that a biomolecule similarly inhibits DPP9 and triggers inflammasome activation during infection, but one has not yet been discovered. Here, we wanted to identify and characterize DPP9-binding proteins to potentially uncover physiologically relevant mechanisms that control DPP9's activity.
View Article and Find Full Text PDFGold(I) complexes of the type [AuL{κC-2-CHP(S)Ph}] [L = PTA, PPh, PPh(CH-3-SONa) and PPh(2-py)]: Synthesis, characterisation, crystal structures, and In Vitro and In Vivo anticancer properties.
Eur J Med Chem
January 2025
School of Science, STEM College, RMIT University, Melbourne, Victoria, 3001, Australia. Electronic address:
Four new mononuclear gold (I) compounds of the type [AuL{κC-2-CHP(S)Ph}] {L = PTA (1), PPh (2), PPh(CH-3-SONa) (3), and PPh(2-py) (4)} were prepared by scission of the dinuclear compound [Au{μ-2-CHP(S)Ph}] by L or via a transmetalation reaction using the organotin reagent 2-MeSnCHP(S)Ph and a suitable gold halide precursor. The cytotoxic potential of complexes 1-4 was evaluated against four human cancer cell lines of diverse cellular origin: cervical (HeLa), prostate (PC-3), non-small cell lung adenocarcinoma (A549), and fibrosarcoma (HT-1080). The in vitro cytotoxicity results showed that 1 demonstrated exceptional anticancer activity with IC values ranging from 0.
View Article and Find Full Text PDFMetformin modulates the TXNIP-NLRP3-GSDMD pathway to improve diabetic bladder dysfunction.
Sci Rep
October 2024
Urology Department of General Hospital, Ningxia Medical University, Yinchuan, Ningxia, China.
Article Synopsis
- The study aimed to evaluate the effectiveness of metformin in treating diabetic bladder dysfunction (DBD) and investigate its mechanism involving the TXNIP-NLRP3-GSDMD pathway.
- C57BL/6J mice were placed on a high-fat diet to induce obesity, then treated with metformin, which led to improved glucose metabolism and positive changes in bladder function, including reduced urination frequency.
- Metformin treatment restored bladder tissue structure and protein levels, indicating it helps protect against urothelial cell damage by inhibiting specific pyroptotic factors associated with DBD.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!