AI Article Synopsis
- The study investigates the role of helix P4 in the RNase P ribozyme's catalytic function, specifically its interaction with magnesium ions essential for activity.
- Researchers found that the universally conserved bulge of helix P4, despite being located away from the cleavage site, can still influence how metal ions bind to the active site.
- The findings suggest that helix P4 helps in positioning the substrate relative to the active site, which is crucial for the effective binding of catalytic metal ions.
Article Abstract
Although helix P4 in the catalytic domain of the RNase P ribozyme is known to coordinate magnesium ions important for activity, distinguishing between direct and indirect roles in catalysis has been difficult. Here, we provide evidence for an indirect role in catalysis by showing that while the universally conserved bulge of helix P4 is positioned 5 nt downstream of the cleavage site, changes in its structure can still purturb active site metal binding. Because changes in helix P4 also appear to alter its position relative to the pre-tRNA cleavage site, these data suggest that P4 contributes to catalytic metal ion binding through substrate positioning.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1524898 | PMC |
| http://dx.doi.org/10.1261/rna.158606 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Self-Assembled Lubricin (PRG-4)-Based Biomimetic Surface-Enhanced Raman Scattering Sensor for Direct Droplet Detection of Melamine in Undiluted Milk.
Biosensors (Basel)
December 2024
Department of Biochemistry and Chemistry, La Trobe University, Bundoora, VIC 3086, Australia.
Surface-enhanced Raman scattering (SERS) is a powerful optical sensing platform that amplifies the target signals by Raman scattering. Despite SERS enabling a meager detection limit, even at the single-molecule level, SERS also tends to equally enhance unwanted molecules due to the non-specific binding of noise molecules in clinical samples, which complicates its use in complex samples such as bodily fluids, environmental water, or food matrices. To address this, we developed a novel non-fouling biomimetic SERS sensor by self-assembling an anti-adhesive, anti-fouling, and size-selective Lubricin (LUB) coating on gold nanoparticle (AuNP) functionalized glass slide surfaces via a simple drop-casting method.
View Article and Find Full Text PDFBiomimetic [MFeS] Cubanes (M = V/Mo) as Catalysts for a Fischer-Tropsch-like Hydrocarbon Synthesis─A Computational Study.
Inorg Chem
December 2024
Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.
Nitrogenase is the enzyme primarily responsible for reducing atmospheric nitrogen to ammonia. There are three general forms of nitrogenase based on the metal ion present in the cofactor binding site, namely, molybdenum-dependent nitrogenases with the iron-molybdenum cofactor (FeMoco), the vanadium-dependent nitrogenases with FeVco, and the iron-only nitrogenases. It has been shown that the vanadium-dependent nitrogenases tend to have a lesser efficacy in reducing dinitrogen but a higher efficacy in binding and reducing carbon monoxide.
View Article and Find Full Text PDFSafety and Phosphate-Binding Capacity of Oxylanthanum Carbonate in Healthy Volunteers.
Clin Transl Sci
January 2025
University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Despite the widespread use of currently available serum phosphate management options, elevated serum phosphate is common in patients with end-stage kidney disease on dialysis. Characteristics of currently available phosphate binders that lead to poor patient experiences such as large drug volume size of required daily medication (e.g.
View Article and Find Full Text PDFPerR functions as a redox-sensing transcription factor regulating metal homeostasis in the thermoacidophilic archaeon Saccharolobus islandicus REY15A.
Nucleic Acids Res
December 2024
CRISPR and Archaea Biology Research Center, State Key Laboratory of Microbial Technology, Microbial Technology Institute, Shandong University, 266237 Qingdao, China.
Thermoacidophilic archaea thrive in environments with high temperatures and low pH where cells are prone to severe oxidative stress due to elevated levels of reactive oxygen species (ROS). While the oxidative stress responses have been extensively studied in bacteria and eukaryotes, the mechanisms in archaea remain largely unexplored. Here, using a multidisciplinary approach, we reveal that SisPerR, the homolog of bacterial PerR in Saccharolobus islandicus REY15A, is responsible for ROS response of transcriptional regulation.
View Article and Find Full Text PDFFine-Modulation of Perovskite Ion-Additive Binding Interaction Using Multidentate Ligation for High Performance Perovskite Light-Emitting Diodes.
ACS Nano
December 2024
Department of Chemistry, Korea University, Seoul 02841, Republic of Korea.
Research on perovskite light-emitting diodes (PeLEDs) has primarily focused on modulating crystal growth to achieve smaller grain sizes and defect passivation using organic additives. However, challenges remain in controlling the intermolecular interactions between these organic additives and perovskite precursor ions for precise modulation of crystal growth. In this study, we synthesize two triphenylphosphine oxide (TPPO)-based multidentate additives: bidentate hexane-1,6-diyl-bis(oxy-4-triphenylphosphine oxide) (2-TPPO) and tetradentate pentaerythrityl-tetrakis(oxy-4-triphenylphosphine oxide) (4-TPPO).
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!