CISD3 is a mitochondrial protein belonging to the NEET proteins family, bearing two [FeS] clusters coordinated by CDGSH domains. At variance with the other proteins of the NEET family, very little is known about its structure-function relationships. NMR is the only technique to obtain information at the atomic level in solution on the residues involved in intermolecular interactions; however, in paramagnetic proteins this is limited by the broadening of signals of residues around the paramagnetic center. Tailored experiments can revive signals of the cluster surrounding; however, signals identification without specific residue assignment remains useless. Here, we show how paramagnetic relaxation can drive the signal assignment of residues in the proximity of the paramagnetic center(s). This allowed us to identify the potential key players of the biological function of the CISD3 protein.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.jinorgbio.2022.112089 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Molecular Interactions between Tau Protein and TIA1: Distinguishing Physiological Condensates from Pathological Fibrils.
ACS Chem Neurosci
October 2024
School of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram (IISER TVM), Vithura, Thiruvananthapuram 695551, India.
Article Synopsis
- The study explores how tau protein interacts with stress granule protein TIA1, which is crucial for understanding their roles in stress responses and conditions like Alzheimer's.
- Researchers investigated two forms of TIA1: the full-length condensate and low complexity domain fibrils, and how these forms affect tau protein dynamics.
- Findings revealed that tau's interactions with TIA1 differ significantly depending on whether TIA1 is in its normal or pathological state, highlighting the complexity of protein interactions in cellular stress responses.
Understanding β-strand mediated protein-protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification.
Chem Sci
July 2024
Astbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK
A significant challenge in chemical biology is to understand and modulate protein-protein interactions (PPIs). Given that many PPIs involve a folded protein domain and a peptide sequence that is intrinsically disordered in isolation, peptides represent powerful tools to understand PPIs. Using the interaction between small ubiquitin-like modifier (SUMO) and SUMO-interacting motifs (SIMs), here we show that -methylation of the peptide backbone can effectively restrict accessible peptide conformations, predisposing them for protein recognition.
View Article and Find Full Text PDFQuantitative analysis of the slow exchange process by F NMR in the presence of scalar and dipolar couplings: applications to the ribose 2'-F probe in nucleic acids.
J Biomol NMR
December 2024
Laboratory for Dynamic Structure of Biomolecules, RIKEN Center for Biosystems Dynamics Research (BDR), 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.
Solution NMR spectroscopy is a particularly powerful technique for characterizing the functional dynamics of biomolecules, which is typically achieved through the quantitative characterization of chemical exchange processes via the measurement of spin relaxation rates. In addition to the conventional nuclei such as N and C, which are abundant in biomolecules, fluorine-19 (F) has recently garnered attention and is being widely used as a site-specific spin probe. While F offers the advantages of high sensitivity and low background, it can be susceptible to artifacts in quantitative relaxation analyses due to a multitude of dipolar and scalar coupling interactions with nearby H spins.
View Article and Find Full Text PDFMRI-based virtual pathology of the prostate.
MAGMA
August 2024
Department of Radiodiagnosis, King George's Medical University, Lucknow, India.
Prostate cancer poses significant diagnostic challenges, with conventional methods like prostate-specific antigen (PSA) screening and transrectal ultrasound (TRUS)-guided biopsies often leading to overdiagnosis or miss clinically significant cancers. Multiparametric MRI (mpMRI) has emerged as a more reliable tool. However, it is limited by high inter-observer variability and radiologists missing up to 30% of clinically significant cancers.
View Article and Find Full Text PDFMobility of sodium ions in agarose gels probed through combined single- and triple-quantum NMR.
Methods
August 2024
Heinrich Heine University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Physical Biology, Universitätsstraße 1 D-40225 Düsseldorf, Germany; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich D-52428 Jülich, Germany. Electronic address:
Metal ions, including biologically prevalent sodium ions, can modulate electrostatic interactions frequently involved in the stability of condensed compartments in cells. Quantitative characterization of heterogeneous ion dynamics inside biomolecular condensates demands new experimental approaches. Here we develop a Na NMR relaxation-based integrative approach to probe dynamics of sodium ions inside agarose gels as a model system.
View Article and Find Full Text PDFWant 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!