Researchers have discovered the process of incorporating selenium into 25 specialized proteins, essential for various cellular and metabolic processes. The study provides critical insights into the workings of these vital mechanisms, which could lead to the development of new medical therapies.
Scientists at Karolinska Institutet and Stockholm University have visualized the machinery that mitochondria use to form their proteins. This discovery presents opportunities to design more specific antibiotics and cancer drugs.
A gene associated with Nascimento Syndrome triggers cells' defenses against environmental attacks by modifying proteins under stress. Rad6, a master regulator of this process, helps cells adapt to stressful conditions, shedding light on the disease's progression.
Researchers found that a common asthma medication can bind to and block the Nsp1 protein of SARS-CoV-2, preventing it from shutting down vital proteins in human immune cells. The study suggests that targeting this region could be an effective way to reduce damage inflicted by the virus.
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Researchers studied peptide bond formation between tRNA molecules and a ribosomal RNA segment, revealing the potential for minihelices to bind to the primordial peptidyl transferase center. The study suggests that functional interactions between tRNA and PTC could have been 'revised' in evolution.
Researchers at UT Southwestern identified a four-protein complex crucial for ribosome production, shedding light on the process of ribosome biogenesis. The findings may lead to new treatments for conditions like cancer, ribosomopathies, and neurodevelopmental disorders.
Autophagy is induced when ER-bound ribosomes are stalled, rescuing them from cellular harm. The ERC grant aims to decipher the role of Autophagy in rescuing stalled ER-bound ribosomes.
A team of researchers has identified a bacterial protein called MutS2 that detects stalled ribosomes and marks them for destruction. The discovery sheds light on the fundamental process of quality control in bacteria, which may also play a role in neurodegenerative diseases in humans.
In bacteria, ribosome collisions trigger the rescue operation by detecting and eliminating defective mRNA and proteins. The SmrB enzyme plays a crucial role in this process, scanning normally translating ribosomes and cutting problematic mRNA upon collision.
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Researchers have discovered how bacteria clean up after molecular crashes, revealing a universal rescue mechanism that works in both bacteria and yeast. The study identifies a molecule called SmrB as the key player in this process.
A research team has discovered how the Covid virus reproduces itself by taking over the cell's protein factory. The team identified a specific structure in viral mRNA that allows the virus to access the ribosome and produce its own proteins, while blocking cellular production. This discovery opens up new avenues for antiviral treatments.
An international research team found that the protein complex NAC acts as a 'gatekeeper' controlling protein transport to the endoplasmic reticulum. NAC prevents non-specific binding of SRP to ribosomes, ensuring only proteins with ER destination are transported. This sorting mechanism ensures cellular function and viability.
A genome study found significant variation in human ribosomal RNA (rRNA) genes based on geographic ancestry, particularly in the 28S rRNA segment. This discovery suggests that these variants may be important for understanding cancer development and functionally assessing their impact on ribosome functions.
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Aging leads to protein misfolding, which overwhelms the cell's quality control system. Ribosome dysfunction causes a snowball effect of dysfunction, leading to disease. Insights from yeast and roundworm models suggest a two-pronged situation where aging increases stalling and collisions, but the safety net is lost.
Researchers at Penn State will investigate ways to stimulate muscle growth by increasing ribosome production. Their goal is to find molecular targets that can be used to promote muscle growth without exercise or drugs. This study aims to prevent muscle loss due to aging, cancer, and other chronic diseases.
Scientists at Baylor College of Medicine identified two rare inherited vitamin B12 conditions that share the same gene but exhibit distinct clinical features. The study found that additional genes, including RONIN and HCFC1, are affected, leading to a more complex syndrome.
University of Michigan scientists found that RNAs associated with an understudied cell compartment in hippocampal neurons vary greatly between sleeping and sleep-deprived mice after learning. These changes are present almost exclusively on ribosomes associated with neuronal cell membranes, suggesting a novel mechanism for memory storage.
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Researchers discovered that chemotherapy drugs can affect protein synthesis in muscle cells, even at low doses. This finding has significant implications for cancer treatment and exercise rehabilitation programs, suggesting that even non-oxidative stress effects of chemotherapy should be considered.
Researchers used a yeast model to understand the dynamics of early-stage ribosomal subunit assembly, discovering snR190 functions as an RNA chaperone. The study also identified Dbp7 as the enzyme responsible for dissociating snR190 from ribosomal RNA precursors.
A new study reveals that iboxamycin effectively fights both gram-negative and gram-positive drug-resistant bacteria in mouse models. The researchers discovered the molecular mechanism that allows this drug to overcome resistance, which is important for developing new antibiotics.
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Researchers at the University of Bonn have successfully filmed the nuclear export of protein-building machines, or ribosomes, from the nucleus to the rest of the cell. The study provides new insights into this complex process, which is crucial for understanding how cells produce proteins.
Research reveals how genetic mutations in aminoacyl-tRNA synthetases cause CMT by halting protein production and inducing integrated stress response. The study's findings provide new avenues for therapies against the disease.
Researchers capture detailed images of ribosome assembly using a novel gene-editing platform, providing insights into the role of 70 assembly factors and their impact on rare human diseases. The study reveals three stages of the small subunit formation process.
A new study by UIC researchers shows that antibiotics designed for bacteria can also inhibit protein synthesis in human cells, potentially treating diseases like cancer and neurodegenerative disorders. The team engineered yeast ribosomes to be more bacterial-like, allowing them to respond to macrolide antibiotics.
A team of researchers from ETH Zurich has identified the crucial step in viral protein synthesis that makes coronaviruses like SARS-CoV-2 vulnerable to inhibition. They found that targeting this process with chemical compounds could lead to effective antiviral drugs, offering new hope for treating COVID-19 and other coronaviruses.
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Scientists at Uppsala University resurrected 3.3 billion-year-old bacterial proteins to study their properties and evolutionary history. The researchers found that these ancient proteins had broader specificities than modern counterparts and could function with various types of ribosomes.
Researchers at Children's Hospital of Philadelphia have identified genes responsible for hematopoietic stem cell regeneration via ribosome assembly. This finding enhances our understanding of the importance of proper ribosome assembly in stem cell regeneration and identifies possible targets for future therapies for ribosomopathies, ch...
A new study published in Nature Communications shows that the mutated huntingtin protein slows brain cells' protein-building machines, called ribosomes, by two to four-fold. This slowing effect ultimately leads to cell death in Huntington's disease.
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Researchers at UNC-Chapel Hill develop collaborative strategy to test hypothesis on how tiny chemicals formed basic biochemistry four billion years ago. They aim to enhance understanding of cellular processes to detect new disease treatment strategies and inspire life outside Earth.
Scientists at Charité - Universitätsmedizin Berlin have identified a promising target for new antibacterial agents in the formation of ribosomal components. The study, published in Molecular Cell, reveals that a helper protein called ObgE plays a key role in guiding the process, which could be inhibited to stop bacterial growth.
An international collaboration has captured ribosomes translating messenger RNA from the maternally inherited mitochondrial genome, revealing a novel gating mechanism that prevents premature protein misfolding. This breakthrough uses cryo-electron microscopy to investigate protein folding processes at unprecedented resolution.
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A recent study published in the EMBO Journal has provided new insights into the formation of mitoribosomes, revealing a complex network of assembly factors that shield the sensitive ribosomal core. The researchers identified five key assembly factors that are conserved across different species, including humans.
Scientists observed disulphide bridge formation in ribosomal exit tunnel during protein synthesis, challenging previous assumptions. The discovery sheds new light on the causes of lens opacities and cataracts, a leading cause of vision loss worldwide.
A new machine-learning algorithm reveals multiple possible conformations of proteins that can be determined experimentally using cryo-electron microscopy. The researchers used this technique to study ribosome assembly and identified a new ribosomal state, as well as visualized large-scale flexible motions of the spliceosome.
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Researchers found that hypoxia upregulates RNA polymerase I activity and alters ribosomal RNA methylation patterns, leading to the creation of specialized ribosomes that can differentially regulate translation of specific messenger RNAs. The study supports a long-debated postulate that ribosomal protein factories can be reprogrammed in...
Researchers have discovered that cancer progression leads to fewer skeletal muscle ribosomes, resulting in muscle wasting. The findings suggest a new mechanism for muscle loss that could be relevant not just for people with cancer but also other conditions such as aging and malnutrition.
A new study reveals that a single water molecule is essential for the binding of macrolide antibiotics to bacterial ribosomes, explaining why resistant bacteria are immune to these drugs. This discovery offers a promising lead in developing new antibiotics that do not require this water molecule for binding.
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Researchers use high-speed atomic force microscopy to visualize the structural dynamics and factor pooling of ribosome stalk proteins, shedding light on the translational GTPase factor mechanism. The study reveals two conformations of the stalk protein and provides evidence for a potential role in further stages of protein synthesis.
Researchers at Charité Universitätsmedizin Berlin have visualized the structure of ribosomes in nerve cells at near-atomic resolution, revealing a new key factor Ebp1 controlling brain development and protein synthesis. This study provides insights into the regulatory processes involved in maintaining neuronal proteostasis.
Researchers discovered that melanoma cells employ 'frameshifting' to starve themselves of tryptophan, a key amino acid needed for protein production. This process allows cancer cells to survive and evade T cell attacks.
Cells use ribosomes as sensors to alert them about changes in their environment, triggering quality control responses to resolve collisions. When many ribosomes collide, cells shut down the entire translation system to prevent premature activation of the integrated stress response.
Researchers have uncovered new details of human ribosome maturation, revealing a crucial step in protein synthesis. The study identifies key enzymes and proteins involved in the final trimming step, which is essential for producing functional ribosomes.
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Researchers at Colorado State University have developed a color-coded biosensor that visualizes viral translation in living cells, revealing how viruses hijack host cell protein-making machinery. This breakthrough technology provides unprecedented insight into predicting and controlling viral diseases, including COVID-19.
Researchers at LMU Munich uncover 'molting' process of 90S precursor to small 40S subunit, shedding Russian doll analogy on ribosome maturation. The study sheds new light on the complex process of protein synthesis and its importance in maintaining cellular equilibrium.
Researchers at ETH Zurich have developed a method to determine how tightly ribosomes bind to hundreds of thousands of RNA sequences in a single experiment, using machine learning and deep sequencing technology. This approach enables precise control over protein production in bacteria, with potential applications in genetic diseases.
Researchers analyzed 200 bacterial strains' genomes to determine which ribosomal proteins are essential for a working ribosome. They found that only nine proteins were completely conserved, while 48 were lost in at least one strain, suggesting a non-random pattern of loss.
Researchers at Johns Hopkins Medicine found that a next-generation cholesterol-lowering drug can lower blood cholesterol to safer levels faster when added to traditional therapies. The study showed significant reductions in LDL cholesterol during hospitalization and within a month following a heart attack, suggesting the drug is safe a...
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The study reveals that SARS-CoV-2 protein Nsp1 effectively shuts down the host's anti-viral immune response by binding to the ribosome and preventing protein production. This finding highlights the importance of targeting the interaction between Nsp1 and the ribosome as a potential therapeutic strategy.
A new study reveals that nutrient-starved cells do not preferentially recycle ribosomes through autophagy, but instead degrade a small number of other organelles. Cells have mechanisms to control what they recycle, allowing them to maintain essential building blocks under limited nutrients.
Researchers found that RNA polymerase II enables ribosomal RNA gene expression, a key step in creating molecular complexes that produce proteins in all cells. The enzyme generates R-loops to shield these genes from disruptors produced by Pol I.
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Researchers developed ribosome tethering tools to image neural circuits with greater precision. This allows for direct visualization of neuronal activity, reducing background fluorescence and spurious signals from surrounding nerve fibers.
Scientists at Kazan Federal University identify a unique post-translational modification in Staphylococcus aureus elongation factor P protein. This discovery provides a promising target for developing new antibiotics to combat nosocomial infections.
Scientists found rare codons at the beginning of a sequence do not enhance translation, contrary to previous hypotheses. However, additional start codons and specific sequences like Shine-Dalgarno boxes are beneficial for efficient translation.
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Scientists at the Weizmann Institute of Science have successfully self-synthesized and assembled a ribosome subunit on a surface chip. The discovery opens up new possibilities for designing and testing complex molecular structures, including potential applications in vaccine development and drug production.
The Ccr4-Not complex plays a crucial role in controlling protein production by degrading faulty mRNA. Defects in this complex may lead to incorrect protein concentrations, locations, or shapes, associated with various diseases including Alzheimer's.
The study found that an mRNA molecule's lifetime is correlated with the rate of protein synthesis, and a key protein complex plays a crucial role in this process. The researchers used cryo-electron microscopy to identify the molecular basis for the link between mRNA degradation and ribosomal efficiency.
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Researchers from Kazan Federal University and their international partners have discovered how Staphylococcus aureus resists antibiotics using cryoelectron microscopy and X-ray diffraction. The RsfS protein protects the bacteria by preventing ribosome formation.
Synthetic biology researchers at Northwestern University have created a system that can rapidly create cell-free ribosomes in a test tube, then select the ribosome that can perform a certain function. This platform could help enable new manufacturing approaches to sustainable materials and targeted therapies.
Dr. Shakirov and collaborators identified genes NOP2A, RPL5A, and RPL5B as crucial for controlling telomere length in Arabidopsis thaliana, a small flowering plant. This discovery provides new insights into the connection between ribosome biogenesis and telomere length control.
Researchers clarify how RNA molecules fold during assembly of ribosomes, a complex process previously believed to be tightly controlled. The discovery opens up possibilities for designing targeted antibiotics with fewer side effects and better understanding of cancer growth.