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SLC29A1 and SLC29A2 are human nicotinamide cell membrane transporters.
Nat Commun
January 2025
College of Pharmaceutical Sciences, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou, China.
Nicotinamide (NAM), a main precursor of NAD+, is essential for cellular fuel respiration, energy production, and other cellular processes. Transporters for other precursors of NAD+ such as nicotinic acid and nicotinamide mononucleotide (NMN) have been identified, but the cellular transporter of nicotinamide has not been elucidated. Here, we demonstrate that equilibrative nucleoside transporter 1 and 2 (ENT1 and 2, encoded by SLC29A1 and 2) drive cellular nicotinamide uptake and establish nicotinamide metabolism homeostasis.
View Article and Find Full Text PDFN7-methylguanosine modification in cancers: from mechanisms to therapeutic potential.
J Hematol Oncol
January 2025
Department of Gynecology, Xiangya Hospital, Central South University, Changsha, 410008, Hunan, China.
N7-methylguanosine (m7G) is an important RNA modification involved in epigenetic regulation that is commonly observed in both prokaryotic and eukaryotic organisms. Their influence on the synthesis and processing of messenger RNA, ribosomal RNA, and transfer RNA allows m7G modifications to affect diverse cellular, physiological, and pathological processes. m7G modifications are pivotal in human diseases, particularly cancer progression.
View Article and Find Full Text PDFBicyclic nucleoside analogues: synthesis of thiazolopyrimidine-based nucleosides a copper-catalysed tandem reaction of 5-iodocytidine with isothiocyanates.
Org Biomol Chem
January 2025
Chemical Sciences and Technology Division, CSIR-National Institute for Interdisciplinary Science and Technology (CSIR-NIIST), Thiruvananthapuram 695019, India.
We have devised a copper-catalysed tandem annulation reaction to generate a new class of bicyclic nucleoside analogues (BCNAs), namely, amino-substituted thiazolopyrimidine ribonucleosides. The reaction between triacetyl-5-iodo-cytidine and an appropriate organic isothiocyanate in the presence of a Cu salt and ligand resulted in the formation of an amino-substituted thiazolopyrimidine moiety. This reaction was found to be compatible with a range of aliphatic and aromatic isothiocyanates, affording the corresponding products in moderate to good yields.
View Article and Find Full Text PDFSelection of initiator tRNA and start codon by mammalian mitochondrial initiation factor 3 in leaderless mRNA translation.
Nucleic Acids Res
January 2025
Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5, Kashiwanoha, Kashiwa-shi, Chiba 277-8562, Japan.
Article Synopsis
- The mammalian mitochondrial protein synthesis system is responsible for synthesizing 13 crucial subunits for energy production, but the exact role of IF-3mt in translation initiation is still unclear.
- Researchers created a mitochondrial translation system to explore IF-3mt's proofreading abilities, revealing it helps distinguish between different start codons for more accurate protein synthesis.
- The findings indicate that IF-3mt not only supports initiation from standard AUG start codons but can also facilitate initiation from non-AUG codons like AUA, highlighting its adaptability in working with leaderless mRNAs.
The C-terminal structure of the N6-methyladenosine deaminase YerA and its role in deamination.
Biochem J
January 2025
The Sun Yat-Sen University, Guangzhou, China.
The N6-methyladenine (6mA) modification is an essential epigenetic marker and plays a crucial role in processes, such as DNA repair, replication, gene expression regulation, etc. YerA from Bacillus subtilis is considered a novel class of enzymes capable of catalyzing the deamination of 6mA to produce hypoxanthine. Despite the significance of this type of enzymes in bacterial self-defense systems and potential applications as a gene-editing tool, the substrate specificity, the catalytic mechanism and the physiological function of YerA are currently unclear due to the lack of structural information.
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