Mitochondrial protein heterogeneity stems from the stochastic nature of co-translational protein targeting in cell senescence.

A decline in mitochondrial function is a hallmark of aging and neurodegenerative diseases. It has been proposed that changes in mitochondrial morphology, including fragmentation of the tubular mitochondrial network, can lead to mitochondrial dysfunction, yet the mechanism of this loss of function is unclear. Most proteins contained within mitochondria are nuclear-encoded and must be properly targeted to the mitochondria.

Efficient Prediction Model of mRNA End-to-End Distance and Conformation: Three-Dimensional RNA Illustration Program (TRIP).

The secondary and tertiary structures of RNA play a vital role in the regulation of biological reactions. These structures have been experimentally studied through in vivo and in vitro analyses, and in silico models have become increasingly accurate in predicting them. Recent technologies have diversified RNA structure predictions, from the earliest thermodynamic and molecular dynamic-based RNA structure predictions to deep learning-based conformation predictions in the past decade.

Antimicrobial research of carbohydrate polymer- and protein-based hydrogels as reservoirs for the generation of reactive oxygen species: A review.

Reactive oxygen species (ROS) play an important role in biological milieu. Recently, the rapid growth in our understanding of ROS and their promise in antibacterial applications has generated tremendous interest in the combination of ROS generators with bulk hydrogels. Hydrogels represent promising supporters for ROS generators and can locally confine the nanoscale distribution of ROS generators whilst also promoting cellular integration via biomaterial-cell interactions.

Single-chain models illustrate the 3D RNA folding shape during translation.

The three-dimensional conformation of RNA is important in the function and fate of the molecule. The common conformation of mRNA is formed based on the closed-loop structure and internal base pairings with the activity of the ribosome movements. However, recent reports suggest that the closed-loop structure might not be formed in many mRNAs.

Post-transcriptional control of mitochondrial protein composition in changing environmental conditions.

In fluctuating environmental conditions, organisms must modulate their bioenergetic production in order to maintain cellular homeostasis for optimal fitness. Mitochondria are hubs for metabolite and energy generation. Mitochondria are also highly dynamic in their function: modulating their composition, size, density, and the network-like architecture in relation to the metabolic demands of the cell.

Mitochondrial volume fraction and translation duration impact mitochondrial mRNA localization and protein synthesis.

Mitochondria are dynamic organelles that must precisely control their protein composition according to cellular energy demand. Although nuclear-encoded mRNAs can be localized to the mitochondrial surface, the importance of this localization is unclear. As yeast switch to respiratory metabolism, there is an increase in the fraction of the cytoplasm that is mitochondrial.

The tRNA Splicing Endonuclease Complex Cleaves the Mitochondria-localized CBP1 mRNA.

The tRNA splicing endonuclease (Sen) complex is located on the mitochondrial outer membrane and splices precursor tRNAs in Saccharomyces cerevisiae. Here, we demonstrate that the Sen complex cleaves the mitochondria-localized mRNA encoding Cbp1 (cytochrome b mRNA processing 1). Endonucleolytic cleavage of this mRNA required two cis-elements: the mitochondrial targeting signal and the stem-loop 652-726-nt region.

Roles of dom34:hbs1 in nonstop protein clearance from translocators for normal organelle protein influx.

Because messenger RNAs without a stop codon (nonstop mRNAs) generate stalled ribosomes, cells have developed a mechanism allowing degradation of nonstop mRNAs and their translation products (nonstop proteins) in the cytosol. Here, we observe the fate of nonstop proteins destined for organelles such as the endoplasmic reticulum (ER) and mitochondria. Nonstop mRNAs for secretory-pathway proteins in yeast generate nonstop proteins that become stuck in the translocator, the Sec61 complex, in the ER membrane.

Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3' end of aberrant mRNA.

Translation arrest leads to an endonucleolytic cleavage of mRNA that is termed no-go decay (NGD). It has been reported that the Dom34:Hbs1 complex stimulates this endonucleolytic cleavage of mRNA induced by translation arrest in vivo and dissociates subunits of a stalled ribosome in vitro. Here we report that Dom34:Hbs1 dissociates the subunits of a ribosome that is stalled at the 3' end of mRNA in vivo, and has a crucial role in both NGD and nonstop decay.

Tethering of poly(A)-binding protein interferes with non-translated mRNA decay from the 5' end in yeast.

The decay of eukaryotic mRNA is triggered mainly by deadenylation, which leads to decapping and degradation from the 5' end of an mRNA. Poly(A)-binding protein has been proposed to inhibit the decapping process and to stabilize mRNA by blocking the recruitment of mRNA to the P-bodies where mRNA degradation takes place after stimulation of translation initiation. In contrast, several lines of evidence show that poly(A)-binding protein (Pab1p) has distinct functions in mRNA decay and translation in yeast.