98%
921
2 minutes
20
Mitochondrially generated ROS increase with age and are a major factor that damages proteins by oxidative modification. Accumulation of oxidatively damaged proteins has been implicated as a causal factor in the age-associated decline in tissue function. Mitochondrial electron transport chain (ETC) complexes I and III are the principle sites of ROS production, and oxidative modifications to their complex subunits inhibit their in vitro activity. We hypothesize that mitochondrial complex subunits may be primary targets for modification by ROS, which may impair normal complex activity. This study of heart mitochondria from young, middle-aged, and old mice reveals that there is an age-related decline in complex I and V activity that correlates with increased oxidative modification to their subunits. The data also show a specificity for modifications of the ETC complex subunits, i.e., several proteins have more than one type of adduct. We postulate that the electron leakage from ETC complexes causes specific damage to their subunits and increased ROS generation as oxidative damage accumulates, leading to further mitochondrial dysfunction, a cyclical process that underlies the progressive decline in physiologic function of the aged mouse heart.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2423468 | PMC |
http://dx.doi.org/10.1016/j.freeradbiomed.2008.01.032 | DOI Listing |
J Neurochem
September 2025
Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Memory formation involves a complex interplay of molecular and cellular processes, including synaptic plasticity mechanisms such as long-term potentiation (LTP) and long-term depression (LTD). These processes rely on activity-dependent gene expression and local protein synthesis at synapses. A central unresolved question in neuroscience is how memories can be stably maintained over time, despite the transient nature of the proteins involved in their initial encoding.
View Article and Find Full Text PDFBMB Rep
September 2025
Department of Molecular Biology, Dankook University, Cheonan 31116, Korea.
Anaphase-promoting complex/cyclosome (APC/C) regulates the cell cycle by destruction of target proteins ubiquitination. However, understanding the control of APC/C has remained elusive. We identify APC2, the catalytic core subunit of APC/C, as a binding partner of active regulator of SIRT1 (AROS).
View Article and Find Full Text PDFPestic Biochem Physiol
November 2025
Julius Kühn Institute (JKI) - Federal Research Centre for Cultivated Plant, Institute for Biosafety in Plant Biotechnology, 06484 Quedlinburg, Germany. Electronic address:
The Colorado potato beetle (CPB, Leptinotarsa decemlineata) is a major pest of solanaceous crops and has developed resistance to many conventional insecticides, highlighting the need for novel, environmentally sustainable control strategies. In this study, we evaluated the efficacy of RNA interference (RNAi) targeting the proteasome subunit β5 (PSMB5) gene as a biopesticide approach against CPB larvae. Double-stranded RNA (dsRNA) targeting PSMB5 (a highly specific dsRNA) and Actin (a less specific dsRNA) dsRNA was synthesized and applied via leaf dip assays, either in naked form or formulated with chitosan nanoparticles.
View Article and Find Full Text PDFPestic Biochem Physiol
November 2025
Key Laboratory of Zoological Systematics and Application of Hebei Province, College of Life Sciences, Hebei University, Baoding, China. Electronic address:
The 20S proteasome is a core component of the ubiquitin-proteasome system, participating in various biological processes such as cell cycle regulation, signal transduction, apoptosis, and protein homeostasis. However, its roles in mammals are well-documented, its function in the insect intestine remains largely unexplored. In this study, we identified 14 20S proteasome subunits, including 7 α-subunits and 7 β-subunits in Locusta migratoria, a worldwide agricultural pest.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Biochemistry and Molecular Biology, Penn State University, University Park, PA, 16802; Center for Structural Biology, Penn State University, University Park, PA 16802; Center for RNA Molecular Biology, Penn State University, University Park, PA 16802. Electronic address:
Despite the overall conservation of ribosomes across all domains of life, differences in their 3D architecture, rRNA sequences, ribosomal protein composition, and translation factor requirements reflect lineage-specific adaptations to environmental niches. In the domain Archaea, structural studies have primarily focused on non-methanogenic thermophiles and halophiles, leaving it unclear whether these represent the broader archaeal domain. Here, we report the cryo-electron microscopy (cryo-EM) structure of the ribosome from Methanosarcina acetivorans, a previously unreported high-resolution structure from a model mesophilic methanogenic archaeon.
View Article and Find Full Text PDF