N -methyladenosine (m A), as the most abundant RNA epigenetic modifications, has been shown to play critical roles in various biological functions. Research about enzymes that can catalyze and remove m A have revealed its comprehensive roles in messenger RNA (mRNA) metabolism and other physiological processes. The "readers" including YTH domain-containing proteins, hnRNPC, hnRNPG, hnRNPA2B1, IGF2BP1, IGF2BP2, and IGF2BP3, which can affect the fates of mRNA in an m A-dependent manner. In this review, we focus on recent advances in the research of the m A modifications, especially about the latest functions of its writers, erasers, readers in RNA metabolism, cancer, and lipid metabolism. In the end, we provide insights into the underlying molecular mechanisms of m A modifications.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1002/jcp.28014 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
Experimental Physics V, Department of Physics, University of Bayreuth, D-95447 Bayreuth, Germany.
Photosynthetic microbes have evolved and successfully adapted to the ever-changing environmental conditions in complex microhabitats throughout almost all ecosystems on Earth. In the absence of light, they can sustain their biological functionalities through aerobic respiration, and even in anoxic conditions through anaerobic metabolic activity. For a suspension of photosynthetic microbes in an anaerobic environment, individual cellular motility is directly controlled by its photosynthetic activity, i.
View Article and Find Full Text PDFInorg Chem
January 2025
Department of Chemistry & CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193 Aveiro, Portugal.
The development of photoresponsive ferroelastics, which couple light-induced macroscopic mechanical and microscopic domain properties, represents a frontier in materials science with profound implications for advanced functional applications. In this study, we report the rational design and synthesis of two new organic-inorganic hybrid ferroelastic crystals, (MA)(MeN)[Fe(CN)(NO)] (MA = methylammonium) () and (MA)(MeNOH)[Fe(CN)(NO)] (), using a dual-organic molecular design strategy that exploits hydrogen-bonding interactions for tailoring ferroelastic properties. Specifically, exhibits a two-step phase transition at 138 and 242 K, while the introduction of a hydroxyl group in stabilizes its ferroelastic phase to a significantly higher temperature, achieving a phase transition at 328 K, 86 K above that of .
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Nanjing University, School of Chemistry and Chemical Engineering, No. 165, Xianlin Road, 210023, Nanjing, CHINA.
Achieving dynamic multicolor emission through solid-state molecular motion is of significant importance for advancing applications in organic solid-state luminescent materials. Herein, we report macrocycle crystals with unique forward‒ and retro‒vapofluorochromic behavior, which is realized by reversible amine vapor uptake and amine‒"squeeze" induced guest release. The forward‒vapofluorochromism occurs when aliphatic amines penetrate guest-free macrocycle crystals to form host‒guest complex crystals.
View Article and Find Full Text PDFFront Vet Sci
January 2025
Jiangsu Agri-animal Husbandry Vocational College, Taizhou, Jiangsu, China.
Introduction: The H9N2 avian influenza virus is widely disseminated in poultry and poses a zoonotic threat, despite vaccination efforts. Mutations at residue 198 of hemagglutinin (HA) are critical for antigenic variation and receptor-binding specificity, but the underlying molecular mechanisms remain unclear. This study explores the molecular mechanisms by which mutations at the HA 198 site affect the antigenicity, receptor specificity, and binding affinity of the H9N2 virus.
View Article and Find Full Text PDFFront Mol Biosci
January 2025
Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY, United States.
This study investigates the dynamics of oleate hydratase (OhyA), a bacterial flavoenzyme from , and its interactions with lipid membranes, focusing on the factors influencing membrane binding and oligomerization. OhyA catalyzes the hydration of unsaturated fatty acids, playing a key role in bacterial pathogenesis by neutralizing host antimicrobial fatty acids. OhyA binds the membrane bilayer to access membrane-embedded substrates for catalysis, and structural studies have revealed that OhyA forms oligomers on membrane surfaces, stabilized by both protein-protein and protein-lipid interactions.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!