This crucial stage in protein synthesis follows initiation, where the ribosome assembles on the mRNA. During this stage, amino acids are sequentially added to the growing polypeptide chain, guided by the codons presented on the mRNA template. Each codon dictates which tRNA, carrying a specific amino acid, will bind to the ribosome. For instance, if the mRNA codon is “AUG,” a tRNA carrying methionine will bind, adding methionine to the nascent protein.
The accuracy and efficiency of this process are paramount for ensuring the proper function of proteins. Errors during this stage can lead to non-functional or even toxic proteins. This highly regulated process involves various elongation factors that facilitate tRNA binding, peptide bond formation, and ribosome translocation along the mRNA. Its efficiency is critical for cellular growth and function, and dysregulation can contribute to various diseases.
The subsequent article will delve deeper into the molecular mechanisms governing this process, exploring the roles of specific elongation factors, quality control mechanisms, and the impact of various inhibitors on its functionality. Understanding these complexities provides insights into potential therapeutic targets for various diseases.
1. tRNA selection
tRNA selection constitutes a pivotal checkpoint within the elongation phase of translation. This process dictates the fidelity of protein synthesis by ensuring the correct amino acid is added to the growing polypeptide chain, corresponding to the mRNA codon presented at the ribosomal A-site. The impact of accurate tRNA selection is direct: correct proteins are synthesized, enabling proper cellular function. Conversely, errors in selection lead to the incorporation of incorrect amino acids, potentially resulting in misfolded, non-functional, or even toxic proteins. The significance is seen in diseases like Cystic Fibrosis where a single amino acid deletion caused by misreading mRNA sequence will causing protein misfold and disease.
The mechanism of tRNA selection involves intricate interactions between the mRNA codon, the anticodon loop of the incoming tRNA, and elongation factors. These factors, such as EF-Tu in bacteria or eEF1A in eukaryotes, bind to the aminoacyl-tRNA and deliver it to the ribosome. GTP hydrolysis provides the energy for this binding and subsequent proofreading steps. The ribosome itself plays a crucial role in discriminating between cognate, near-cognate, and non-cognate tRNAs, primarily through interactions with the minor groove of the codon-anticodon helix. Mismatches in this region destabilize the interaction, leading to rejection of the incorrect tRNA. Certain antibiotics like tetracycline inhibit this step by blocking the A site and preventing the aminoacyl-tRNA from attaching to that site of ribosome.
In summary, tRNA selection is an indispensable component of the elongation phase, directly influencing the accuracy and efficiency of protein synthesis. The process involves a complex interplay of molecular components and rigorous proofreading mechanisms to minimize errors. Understanding the molecular basis of tRNA selection is crucial for comprehending cellular function and has implications for developing therapies targeting translational errors in various diseases.
2. Peptide Bond Formation
Peptide bond formation is the central chemical event occurring during the elongation phase of translation. This process covalently links amino acids, thereby extending the nascent polypeptide chain. Without efficient and accurate peptide bond formation, the synthesis of functional proteins would cease, resulting in cellular dysfunction and ultimately, cell death. This fundamental connection establishes peptide bond formation not merely as a component of the elongation phase, but as its very driving force. The proper execution of this step, catalyzed by the ribosomal peptidyl transferase center, dictates the primary structure of the protein, directly influencing its subsequent folding, function, and stability. For instance, if the mechanism that binds amino acids together is damage or not present, the cells will not be able to grow or produce protein which may cause a variety of disease.
The peptidyl transferase center, located within the large ribosomal subunit, facilitates peptide bond formation through a complex mechanism involving the positioning of the aminoacyl-tRNA in the A-site and the peptidyl-tRNA in the P-site. The amino group of the aminoacyl-tRNA’s amino acid attacks the carbonyl carbon of the peptidyl-tRNA’s amino acid, forming a new peptide bond and transferring the growing polypeptide chain to the tRNA in the A-site. This process occurs with remarkable speed and precision, often occurring multiple times per second. Some macrolide antibiotics, such as erythromycin, inhibit peptide bond formation by binding to the ribosomal tunnel through which the nascent polypeptide exits. By obstructing this exit tunnel, these drugs prevent the growing chain from elongating, effectively halting protein synthesis.
In summary, peptide bond formation is an indispensable process within the elongation phase of translation. Its fidelity and efficiency are essential for the synthesis of functional proteins and cellular survival. Understanding the intricacies of this reaction, including the role of the ribosome and the impact of inhibitors, provides critical insights into fundamental biological processes and potential therapeutic targets for various diseases involving protein synthesis dysregulation. The challenges lie in fully elucidating the dynamic conformational changes within the ribosome during catalysis and developing novel strategies to target aberrant peptide bond formation in disease states.
3. Ribosome Translocation
Ribosome translocation represents a critical step within the elongation phase of translation, serving as the engine that drives the progression of protein synthesis. Without precise and coordinated translocation, the ribosome stalls, halting polypeptide chain extension and leading to premature termination. This process is not simply a passive movement but a highly regulated, energy-dependent event that ensures the sequential reading of mRNA codons.
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Mechanism of Translocation
Translocation is catalyzed by elongation factor G (EF-G) in prokaryotes and eEF2 in eukaryotes, utilizing the energy from GTP hydrolysis. These factors bind to the ribosome and, through conformational changes, physically move the mRNA and the associated tRNAs by one codon. This movement shifts the peptidyl-tRNA from the A-site to the P-site, and the deacylated tRNA from the P-site to the E-site, making the A-site available for the next aminoacyl-tRNA. Failure in EF-G/eEF2 function directly impedes the subsequent addition of amino acids.
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Maintenance of Reading Frame
Accurate translocation is essential for maintaining the correct reading frame during translation. A frameshift, caused by translocation errors, results in the misreading of codons and the incorporation of incorrect amino acids, leading to non-functional or truncated proteins. This is seen in certain genetic disorders where defects in the ribosome’s structure or associated factors cause elevated frameshifting rates.
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Coupling with Peptide Bond Formation
Translocation is tightly coupled with the preceding step of peptide bond formation and the subsequent step of tRNA selection. After peptide bond formation, the ribosome must translocate before another aminoacyl-tRNA can bind to the A-site. This coordination ensures the continuous and sequential addition of amino acids to the growing polypeptide chain. Inhibitors that interfere with translocation, such as fusidic acid, block the binding of EF-G/eEF2, thereby disrupting the entire elongation cycle.
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Ribosomal Conformational Changes
The process of translocation involves significant conformational changes within the ribosome itself. These changes are essential for the movement of tRNAs and the mRNA, and for the binding and activity of EF-G/eEF2. Cryo-electron microscopy studies have revealed the complex choreography of ribosomal movements during translocation, highlighting the dynamic nature of this process.
These interconnected facets of ribosome translocation underscore its indispensable role in the elongation phase of translation. The fidelity and efficiency of this process are crucial for the synthesis of functional proteins and, ultimately, for cellular survival. Disruptions in translocation can have profound consequences, leading to various diseases and highlighting the importance of understanding its intricate mechanisms.
4. Elongation Factors (EFs)
Elongation factors (EFs) are indispensable components of the elongation phase of translation, acting as catalysts and regulators of the complex processes that govern polypeptide chain extension. These proteins facilitate various steps, including tRNA binding, GTP hydrolysis, ribosome translocation, and error correction. Their proper function is paramount for the fidelity and efficiency of protein synthesis.
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tRNA Delivery to the Ribosome
Elongation factors, such as EF-Tu in bacteria and eEF1A in eukaryotes, are responsible for delivering aminoacyl-tRNAs to the ribosomal A-site. They bind to GTP and the aminoacyl-tRNA, forming a ternary complex that interacts with the ribosome. This delivery ensures that the correct tRNA, corresponding to the mRNA codon, is positioned for peptide bond formation. Mutations in EF-Tu/eEF1A that impair tRNA binding can severely inhibit protein synthesis.
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Facilitating GTP Hydrolysis
GTP hydrolysis is crucial for providing the energy required for several steps within the elongation phase, including tRNA selection and ribosome translocation. EFs act as GTPases, accelerating the hydrolysis of GTP to GDP and inorganic phosphate. This hydrolysis triggers conformational changes in the EF and the ribosome, driving the translocation process. Compounds that inhibit GTP hydrolysis by EFs can stall the ribosome and halt protein synthesis.
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Ribosome Translocation Promotion
EF-G in bacteria and eEF2 in eukaryotes promote the translocation of the ribosome along the mRNA by one codon. These factors bind to the ribosome in a GTP-dependent manner and, upon GTP hydrolysis, induce conformational changes that move the tRNAs and the mRNA. This translocation step is essential for bringing the next codon into the A-site for subsequent tRNA binding. Inhibition of EF-G/eEF2 by toxins like diphtheria toxin disrupts this process, leading to cell death.
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Error Correction and Proofreading
Some EFs play a role in proofreading and error correction during translation. They can discriminate between correct and incorrect tRNA-codon interactions, increasing the accuracy of protein synthesis. This proofreading mechanism involves GTP hydrolysis and conformational changes that allow the ribosome to reject incorrect tRNAs before peptide bond formation. Reduced accuracy of EFs leads to increased translational errors and the production of non-functional proteins.
In summary, Elongation factors (EFs) are pivotal for the function of the elongation phase, driving and regulating key events. Their participation ensures that proteins are synthesized accurately and efficiently. Understanding the functions of these factors is critical for elucidating the mechanisms of protein synthesis and for developing therapeutic strategies targeting translational defects in various diseases. A wide range of diseases, including some cancers, exhibit altered EF expression, making them potential targets for pharmacological intervention.
5. Codon Recognition
Codon recognition is fundamental to the elongation phase of translation, serving as the mechanism by which the genetic code is deciphered and the correct amino acid is added to the growing polypeptide chain. This process dictates the accuracy of protein synthesis, ensuring that the amino acid sequence precisely corresponds to the instructions encoded within the mRNA molecule. The fidelity of codon recognition is, therefore, critical for producing functional proteins.
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tRNA Anticodon Interaction
The core of codon recognition lies in the interaction between the mRNA codon and the anticodon loop of the transfer RNA (tRNA). Each tRNA molecule carries a specific amino acid and possesses a unique anticodon sequence complementary to a particular mRNA codon. For example, the codon AUG, which specifies methionine, is recognized by a tRNA with the anticodon UAC. This base-pairing interaction, following the Watson-Crick rules, ensures the correct amino acid is selected based on the mRNA sequence. Deviations from these rules, or wobble base pairing, allow some tRNAs to recognize multiple codons, but the initial match is crucial for initiating the process.
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Ribosomal A-site Environment
The ribosomal A-site (aminoacyl-tRNA binding site) provides the environment where codon-anticodon recognition occurs. The ribosome does not directly participate in the base-pairing itself but stabilizes the interaction and facilitates the proofreading process. The ribosomal RNA within the A-site forms specific contacts with the minor groove of the codon-anticodon helix, allowing the ribosome to discriminate between correct and incorrect pairings. Mismatched base pairs disrupt these contacts, leading to slower binding and increased likelihood of rejection of the tRNA.
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Elongation Factor Mediated Delivery
Elongation factors, such as EF-Tu in prokaryotes and eEF1A in eukaryotes, play a crucial role in codon recognition by delivering aminoacyl-tRNAs to the ribosomal A-site. These factors bind to the tRNA and GTP, forming a ternary complex that interacts with the ribosome. The elongation factor facilitates the initial codon-anticodon interaction and also participates in a proofreading step, where incorrect tRNAs are rejected before GTP hydrolysis occurs. The GTP hydrolysis is essentially an accuracy check point.
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Consequences of Mismatch
Errors in codon recognition, leading to the incorporation of the wrong amino acid, can have significant consequences for protein function. Misincorporation can result in misfolded proteins, reduced enzymatic activity, or even the creation of toxic protein aggregates. The cell employs quality control mechanisms to identify and degrade misfolded proteins, but a high error rate can overwhelm these systems, leading to cellular dysfunction. For instance, certain neurodegenerative diseases are associated with an increased rate of translational errors and protein misfolding.
These facets of codon recognition collectively highlight its central role in the elongation phase of translation. The interplay between the tRNA anticodon, the ribosomal A-site, and elongation factors ensures the accurate translation of the genetic code into the amino acid sequence of proteins. Disturbances in any of these components can lead to translational errors and compromised protein function, underlining the importance of maintaining high fidelity in codon recognition.
6. GTP Hydrolysis in Elongation Phase of Translation
GTP hydrolysis is a critical energy-releasing event integral to multiple steps within the elongation phase of translation. Its role extends beyond mere energy provision, serving as a regulatory mechanism that ensures fidelity and synchronizes the various events necessary for polypeptide chain extension. The following examines key facets of this connection.
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tRNA Selection and Proofreading
Elongation factors, such as EF-Tu in prokaryotes and eEF1A in eukaryotes, utilize GTP hydrolysis to deliver aminoacyl-tRNAs to the ribosomal A-site. Following initial codon recognition, GTP hydrolysis triggers a conformational change in the elongation factor, resulting in its release from the ribosome if the codon-anticodon pairing is correct. If the pairing is incorrect, the slower rate of GTP hydrolysis increases the likelihood that the tRNA will dissociate before peptide bond formation. This kinetic proofreading mechanism enhances the accuracy of translation. For example, mutations in EF-Tu/eEF1A that impair GTP hydrolysis can lead to increased translational errors. Specific antibiotics disrupt GTP hydrolysis to stop tRNA selection.
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Ribosome Translocation
The translocation of the ribosome along the mRNA by one codon is facilitated by elongation factor G (EF-G) in prokaryotes or eEF2 in eukaryotes, which are GTPases. GTP hydrolysis by EF-G/eEF2 provides the energy for the conformational changes required to move the tRNAs and mRNA through the ribosome. This step is essential for making the A-site available for the next aminoacyl-tRNA. Inhibitors of EF-G/eEF2 can stall the ribosome and halt translation by preventing GTP hydrolysis. Any disruption in this activity will result in cell malfunctions.
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Elongation Factor Recycling
Following GTP hydrolysis, elongation factors must be recycled to participate in subsequent rounds of elongation. This recycling process often involves additional factors that facilitate the exchange of GDP for GTP on the elongation factor. For example, EF-Ts facilitates the regeneration of EF-Tu-GTP. Disruptions in these recycling mechanisms can limit the availability of active elongation factors and slow down the overall rate of protein synthesis. Without this regulation, the proteins will not be produce.
These interconnected roles of GTP hydrolysis highlight its indispensable function in the elongation phase of translation. It is not merely a source of energy but a regulatory switch that ensures the accuracy and coordination of the various steps involved in polypeptide chain extension. Understanding the mechanistic details of GTP hydrolysis by elongation factors is crucial for comprehending the complexities of protein synthesis and for developing therapeutic strategies targeting translational defects.
7. mRNA Movement
Messenger RNA (mRNA) movement is an intrinsic component of the elongation phase of translation, the stage in protein synthesis where the polypeptide chain is extended. This process is not merely a passive diffusion but a highly coordinated, directed translocation that ensures each codon is sequentially presented to the ribosome for accurate decoding. Its relevance lies in maintaining the correct reading frame and facilitating the continuous addition of amino acids to the nascent protein.
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Ribosome Translocation
The primary mechanism for mRNA movement during elongation is ribosome translocation. Following the formation of a peptide bond, the ribosome must advance by one codon along the mRNA molecule. This movement is catalyzed by elongation factor G (EF-G) in prokaryotes and eEF2 in eukaryotes, using the energy derived from GTP hydrolysis. For example, if translocation is inhibited, the ribosome stalls, preventing further elongation and leading to premature termination of protein synthesis. Compounds like fusidic acid disrupt EF-G function, thus blocking ribosome translocation and highlighting its essential role.
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Maintenance of the Reading Frame
Accurate mRNA movement is critical for maintaining the correct reading frame. The reading frame is established during initiation and must be preserved throughout elongation to ensure that each codon is correctly translated. A shift in the reading frame, known as a frameshift mutation, results in the misreading of codons and the incorporation of incorrect amino acids. This can lead to the production of non-functional or truncated proteins. The significance of reading frame maintenance is evident in diseases caused by frameshift mutations, such as certain forms of cystic fibrosis, where disruptions in the reading frame lead to a non-functional protein.
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Coupling with tRNA Movement
mRNA movement is tightly coupled with the movement of transfer RNAs (tRNAs) within the ribosome. As the ribosome translocates, the tRNA that was in the A-site moves to the P-site, and the tRNA that was in the P-site moves to the E-site before being released. This coordinated movement ensures that the correct tRNAs are positioned for peptide bond formation and that the ribosome is cleared for the next incoming tRNA. Disruptions in tRNA movement can stall translocation, thereby affecting the overall efficiency of protein synthesis.
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Role of mRNA Structure
The structure of the mRNA itself can influence its movement through the ribosome. Secondary structures, such as stem-loops or hairpins, can impede ribosome translocation if they are located in the path of the ribosome. Unwinding these structures often requires additional energy and the assistance of RNA helicases. The presence of stable secondary structures near the start codon can even prevent ribosome binding and initiation of translation. Therefore, mRNA structure plays a role in regulating the efficiency and accuracy of mRNA movement during elongation.
In conclusion, mRNA movement is a fundamental and tightly regulated aspect of the elongation phase of translation. It is intricately linked to ribosome translocation, maintenance of the reading frame, tRNA movement, and mRNA structure. Understanding the mechanisms and regulation of mRNA movement is crucial for comprehending the overall process of protein synthesis and its importance in cellular function.
8. Quality Control During Elongation
Quality control mechanisms are essential during the elongation phase of translation to ensure the accurate synthesis of proteins and prevent the accumulation of non-functional or harmful polypeptides. These processes monitor various steps within elongation, identifying and resolving errors that may arise during the addition of amino acids to the growing polypeptide chain. Failure of these mechanisms can lead to protein misfolding, aggregation, and cellular dysfunction.
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Codon-Anticodon Recognition Monitoring
Quality control begins with monitoring the fidelity of codon-anticodon interactions. Ribosomes and elongation factors work together to ensure that the correct tRNA binds to the mRNA codon. If a mismatch occurs, the tRNA is rejected, preventing the incorporation of an incorrect amino acid. However, this process is not perfect, and some errors can still occur. For instance, near-cognate tRNAs, which have slight mismatches with the codon, can sometimes be incorporated, leading to amino acid misincorporation. These inaccuracies are counteracted by downstream mechanisms that target the resulting misfolded proteins. An absence of monitoring will lead to cell dysfunction.
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Ribosome Stalling Surveillance
Ribosomes can stall during elongation due to various factors, such as mRNA damage, rare codons, or structural impediments. Stalled ribosomes trigger quality control pathways that either rescue the ribosome or target the incomplete polypeptide for degradation. One such pathway involves the Dom34/Pelota complex, which recognizes stalled ribosomes and promotes their dissociation from the mRNA. This mechanism prevents the continued translation of aberrant mRNAs and the accumulation of incomplete proteins. Disruptions of ribosome rescues will cause an accumulation of aberrant mRNA.
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No-Go Decay (NGD)
No-Go Decay (NGD) is a mRNA surveillance pathway activated when ribosomes stall due to physical blocks or damaged mRNAs. NGD recognizes these stalled ribosomes and triggers endonucleolytic cleavage of the mRNA upstream of the stalled ribosome. This cleavage results in the degradation of the mRNA fragment and the release of the ribosome, preventing further translation of the defective mRNA. Mutations affecting NGD components lead to accumulation of truncated proteins and can be associated with neurological disorders and developmental defects. A malfunction will lead to accumulation of truncated proteins.
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Targeting Misfolded Proteins for Degradation
Despite the quality control mechanisms during elongation, some misfolded proteins inevitably escape detection. These misfolded proteins are subsequently targeted for degradation by the ubiquitin-proteasome system (UPS) or autophagy. Chaperone proteins, such as heat shock proteins (HSPs), assist in the refolding of misfolded proteins, but if refolding is not possible, the proteins are tagged with ubiquitin and degraded by the proteasome. Autophagy is used for the removal of larger protein aggregates and damaged organelles. The balance between protein synthesis and degradation is essential for maintaining cellular homeostasis. If these quality control mechanisms are faulty, the proteins can’t be degrade and will cause a cell malfunctions.
These interconnected quality control pathways highlight the importance of maintaining translational fidelity during the elongation phase. They function to ensure that proteins are synthesized accurately, preventing the accumulation of non-functional or toxic species. Compromising these mechanisms can have severe consequences for cellular health and organismal viability, emphasizing their critical role in preserving protein homeostasis.
Frequently Asked Questions
This section addresses common inquiries regarding the elongation phase of translation, a crucial step in protein synthesis. The goal is to provide clear, concise answers based on current scientific understanding.
Question 1: What factors determine the speed of the elongation phase?
The rate of polypeptide chain elongation is influenced by several factors, including the availability of aminoacyl-tRNAs, the efficiency of elongation factors, the presence of mRNA secondary structures, and the overall energy status of the cell. A limiting supply of any of these will cause a decrease in speed.
Question 2: How does the ribosome ensure the correct amino acid is added during elongation?
The ribosome facilitates accurate codon-anticodon matching between the mRNA and tRNA. Elongation factors also participate in a proofreading process, rejecting incorrectly paired tRNAs before peptide bond formation occurs. The ribosome’s active site will further proofread after each elongation.
Question 3: What happens if the ribosome encounters a rare codon during elongation?
Rare codons, which are less frequently used, can cause ribosome stalling. This stalling can trigger quality control mechanisms, leading to the degradation of the incomplete polypeptide or recruitment of specialized tRNAs to overcome the bottleneck. It can also be a sign that mutations must be made at the ribosome location or a misread.
Question 4: Can the elongation phase be targeted by therapeutic interventions?
Yes, the elongation phase is a target for several antibiotics that inhibit bacterial protein synthesis. These drugs often interfere with elongation factor function or ribosome translocation. The development of new therapeutics targeting elongation is an ongoing area of research.
Question 5: What role do post-translational modifications play in the elongation phase?
While most post-translational modifications occur after translation is complete, some modifications, such as N-terminal acetylation, can begin during the elongation phase, influencing protein folding and stability.
Question 6: How does the cell respond to errors that occur during the elongation phase?
Cells have quality control mechanisms, such as no-go decay and ribosome rescue pathways, that detect and respond to errors during elongation. These mechanisms can trigger the degradation of aberrant mRNAs or the disassembly of stalled ribosomes, preventing the accumulation of non-functional proteins.
The elongation phase of translation is a highly regulated and complex process. A comprehensive understanding of its mechanisms and regulation is essential for comprehending protein synthesis and cellular function.
The following section will delve into the process that terminates the elongation process.
Enhancing Understanding of the Elongation Phase of Translation
The following guidelines are presented to facilitate a deeper comprehension of the elongation phase of translation, a pivotal step in protein biosynthesis.
Tip 1: Focus on the Key Players: The elongation phase hinges on the coordinated action of the ribosome, mRNA, tRNAs, and elongation factors (EFs). A thorough grasp of each component’s role is paramount.
Tip 2: Understand the Three-Step Cycle: The elongation process is cyclical, involving codon recognition, peptide bond formation, and translocation. Conceptualizing this cycle is crucial.
Tip 3: Elongation Factors are Critical Catalysts: EFs are not merely passive participants. They actively facilitate tRNA binding, GTP hydrolysis, and ribosome translocation. Understanding their functions illuminates the process.
Tip 4: Appreciate the Energy Requirements: GTP hydrolysis provides the energy for multiple steps, including tRNA selection and ribosome translocation. Understanding how the process of GTP is hydrolyzed will provide a clearer understanding of the elongation phase.
Tip 5: Consider the Importance of Fidelity: The elongation phase is subject to quality control mechanisms. Error correction and proofreading ensures the accuracy of protein synthesis, preventing accumulation of non-functional or toxic proteins.
Tip 6: Identify Potential Inhibition Points: Various antibiotics and toxins target the elongation phase. Recognizing these can enhance understanding of vulnerabilities in the protein synthesis machinery.
Tip 7: Visualize the Molecular Interactions: Utilize diagrams and animations to visualize the intricate molecular interactions occurring within the ribosome during elongation. For instance, visualizing how EF-Tu delivers tRNA to the A-site will solidify understanding.
These strategies, when employed systematically, will foster a comprehensive understanding of the intricacies of the elongation phase of translation, thereby furthering insights into cellular processes.
The subsequent section will deal with the termination phase in translation.
Conclusion
This exploration has illuminated the essential aspects of the elongation phase of translation. This stage, critical for protein biosynthesis, involves the sequential addition of amino acids to a growing polypeptide chain, guided by mRNA codons and facilitated by various elongation factors. The fidelity of this process, ensured by rigorous quality control mechanisms and energy-dependent steps, determines the accuracy of protein synthesis and, consequently, cellular function.
Further research into the molecular mechanisms governing the elongation phase of translation is vital. A deeper understanding could reveal novel therapeutic targets for diseases linked to translational errors or dysregulation. Continuous investigation is imperative to fully exploit the potential of manipulating this fundamental biological process for medical and biotechnological advancements.
