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A Conserved Lysine in an Ion-Pair with a Catalytic Glutamate Is Critical for U-to-C RNA Editing but Restricts C-to-U RNA Editing.
Biochemistry
January 2025
Department of Chemistry and Biochemistry, California State University Los Angeles, Los Angeles, California 90032, United States.
Plants make pyrimidine base substitutions in organellar mRNAs through the action of sequence-specific nuclear-encoded enzymes. Pentatricopeptide repeat (PPR) proteins are essential for ensuring specificity, while the enzymatic DYW domain is often present at the C-terminus of a PPR protein and dependent on the variant possessing C-to-U and/or U-to-C RNA editing activities. Expression of exogenous DYW-KP variant enzymes in bacteria leads to the modification of RNAs suggestive of U-to-C base changes.
View Article and Find Full Text PDFCo-Translational Deposition of N-Acetyl-L-Lysine in Nascent Proteins Contributes to the Acetylome in Mammalian Cells.
Adv Sci (Weinh)
January 2025
Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Huazhong University of Science and Technology, Wuhan, Hubei, 430030, China.
Article Synopsis
- N-acetyl-L-lysine is common in dietary protein, yet its effects on consumers are largely unknown.
- Research indicates that Lysyl-tRNA synthetase (KARS) integrates this compound into proteins during their synthesis, influencing cellular acetylation levels.
- This process, called co-translational modification (coTM), allows for the acetylation of proteins in ways that differ from traditional post-translational modifications, potentially expanding our understanding of protein regulation in cells.
Roles of Lysyl oxidases (LOX(L)) in pathologic calcification.
Biomed Pharmacother
December 2024
Service of Rheumatology, Department of Musculoskeletal Medicine, Centre Hospitalier Universitaire Vaudois and University of Lausanne, Lausanne, Switzerland. Electronic address:
Calcification of tissues involves the formation and deposition of calcium-containing crystals in the extracellular matrix (ECM). While this process is normal in bones, it becomes pathological when it occurs in cardiovascular and musculoskeletal soft tissues. Pathological calcification (PC) triggers detrimental pathways such as inflammation and oxidative stress, contributing to tissue damage and dysregulated tissue biomechanics, ultimately leading to severe complications and even death.
View Article and Find Full Text PDFAssembly of the Human Multi-tRNA Synthetase Complex Through Leucine Zipper Motifs.
J Mol Biol
December 2024
School of Life Science and Biotechnology, KNU Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of Korea. Electronic address:
Aminoacyl-tRNA synthetases (ARSs) are responsible for the ligation of amino acids to their cognate tRNAs. In human, nine ARSs form a multi-tRNA synthetase complex (MSC) with three ARS-interacting multifunctional proteins (AIMPs). Among the components of MSC, arginyl-tRNA synthetase 1 (RARS1) and two AIMPs (AIMP1 and AIMP2) have leucine zipper (LZ) motifs, which they utilize for their assembly in an MSC.
View Article and Find Full Text PDFPolylactic acid/chitosan-IKVAV Janus film serving as a dual functional platform for spinal cord injury repair.
Nanoscale
December 2024
Department of Neurosurgery, Qilu Hospital, Cheeloo College of Medicine and Institute of Brain and Brain-Inspired Science, Shandong University, Jinan 250100, P. R. China.
The repair of traumatic spinal cord injury (SCI) remains a challenge due to the non-regenerative nature of functional neurons in adults. Neural stem cell (NSC)-based therapy has emerged as a promising approach for the treatment of SCI by replacing the damaged neurons with differentiated stem cells. However, directing the neuronal differentiation of implanted stem cells in the injury microenvironment is of great difficulty, especially considering that SCI is generally associated with severe fibrotic tissue infiltration, neuron inflammation, and tissue adhesion.
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