As ancient bacterial endosymbionts of eukaryotic cells, mitochondria have retained their own circular DNA as well as protein translation system including mitochondrial ribosomes (mitoribosomes). In recent years, methodological advancements in cryoelectron microscopy and mass spectrometry have revealed the extent of the evolutionary divergence of mitoribosomes from their bacterial ancestors and their adaptation to the synthesis of 13 mitochondrial DNA encoded oxidative phosphorylation complex subunits. In addition to the structural data, the first assembly pathway maps of mitoribosomes have started to emerge and concomitantly also the assembly factors involved in this process to achieve fully translational competent particles. These transiently associated factors assist in the intricate assembly process of mitoribosomes by enhancing protein incorporation, ribosomal RNA folding and modification, and by blocking premature or non-native protein binding, for example. This review focuses on summarizing the current understanding of the known mammalian mitoribosome assembly factors and discussing their possible roles in the assembly of small or large mitoribosomal subunits.
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http://dx.doi.org/10.1016/j.mito.2021.07.008 | DOI Listing |
Soft Matter
January 2025
Faculty of Chemistry, Ho Chi Minh City University of Science, Vietnam National University, Ho Chi Minh City, 227 Nguyen Van Cu Street, Ward 4, District 5, Ho Chi Minh City 70000, Vietnam.
Surface-enhanced Raman spectroscopy (SERS) is a highly sensitive analytical technique with excellent molecular specificity. However, separate pristine nanoparticles produce relatively weak Raman signals. It is necessary to focus on increasing the "hot-spot" density generated at the nanogaps between the adjacent nanoparticles (second-generation SERS hotspot), thus significantly boosting the Raman signal by creating an electromagnetic field.
View Article and Find Full Text PDFQ Rev Biophys
January 2025
Instituto Biofisika (CSIC-UPV/EHU), University of the Basque Country (UPV/EHU), Bilbao, Spain.
The 'Viroporin' family comprises a number of mostly small-sized, integral membrane proteins encoded by animal and plant viruses. Despite their sequence and structural diversity, viroporins share a common functional trend: their capacity to assemble transmembrane channels during the replication cycle of the virus. Their selectivity spectrum ranges from low-pH-activated, unidirectional proton transporters, to size-limited permeating pores allowing passive diffusion of metabolites.
View Article and Find Full Text PDFJ Ovarian Res
January 2025
Department of Urology, Zigong Fourth People's Hospital, Zigong, Sichuan, China.
Background: Granulosa cell proliferation and survival are essential for normal ovarian function and follicular development. Long non-coding RNAs (lncRNAs) have emerged as important regulators of cell proliferation and differentiation. Nuclear paraspeckle assembly transcript 1 (NEAT1) has been implicated in various cellular processes, but its role in granulosa cell function remains unclear.
View Article and Find Full Text PDFDiscov Oncol
January 2025
The School Public Health, Fujian Medical University, Fuzhou, 350122, Fujian, China.
The prognosis and treatment efficacy of lung adenocarcinoma (LUAD), a disease with a high incidence, remains unsatisfactory. Identifying new biomarkers and therapeutic targets for LUAD is essential. Chromosomal assembly factor 1B (CHAF1B), a p60 component of the CAF-1 complex, is closely linked to tumor incidence and cell proliferation.
View Article and Find Full Text PDFMethods Mol Biol
January 2025
Quantum-Si, Guilford, CT, USA.
Single-molecule fluorescence resonance energy transfer (smFRET) is a powerful technique for studying the structural dynamics of protein molecules or detecting interactions between protein molecules in real time. Due to the high sensitivity in spatial and temporal resolution, smFRET can decipher sub-populations within heterogeneous native state conformations, which are generally lost in traditional measurements due to ensemble averaging. In addition, the single-molecule reconstitution allows protein molecules to be observed for an extensive period of time and can recapitulate the geometry of the cellular environment to retain biological function.
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