Biochemistry Biochemistry最新文献_第3页

Chemical Identification of [Fe(III)(OH)(H₂O)]²⁺ Complex Ion at the Ferroxidase Active Site in Cryo-EM Maps. [Fe(III)(OH)(H2O)]2+配合物在铁氧化酶活性位点的化学鉴定。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-04-29 DOI: 10.1021/acs.biochem.4c00738

Jimin Wang

引用次数: 0

Multitasking Proteins: Exploring Noncanonical Functions of Proteins during Mitosis. 多任务蛋白质：探索有丝分裂过程中蛋白质的非规范功能。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-02 DOI: 10.1021/acs.biochem.5c00083

Valentina Piano

{"title":"Multitasking Proteins: Exploring Noncanonical Functions of Proteins during Mitosis.","authors":"Valentina Piano","doi":"10.1021/acs.biochem.5c00083","DOIUrl":"10.1021/acs.biochem.5c00083","url":null,"abstract":"This review provides a comprehensive overview of how mitotic cells drive the repurposing of proteins to fulfill mitosis-specific functions. To ensure the successful completion of cell division, the cell strategically reallocates its \"workforce\" by assigning additional functions to available proteins. Protein repurposing occurs at multiple levels of cellular organization and involves diverse mechanisms. At the protein level, proteins may gain mitosis-specific functions through post-translational modifications. At the structural level, proteins that typically maintain cellular architecture in interphase are co-opted to participate in mitotic spindle formation, chromosome condensation, and kinetochore assembly. Furthermore, the dynamic reorganization of the nuclear envelope and other organelles relies on the temporary reassignment of enzymes, structural proteins, and motor proteins to facilitate these changes. These adaptive mechanisms underscore the remarkable versatility of the cellular proteome in responding to the stringent requirements of mitosis. By leveraging the existing proteome for dual or multiple specialized roles, cells optimize resource usage while maintaining the precision needed to preserve genomic integrity and ensure the survival of the next generation of cells.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2123-2137"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955139","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Target Recognition Mechanism of Thermus thermophilus Argonaute at the Supplementary Site. 嗜热热菌Argonaute在辅助位点的靶识别机制。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-09 DOI: 10.1021/acs.biochem.5c00056

Kun Xi, Jinchu Liu, Wenzhuo Ma, Lizhe Zhu

{"title":"Target Recognition Mechanism of Thermus thermophilus Argonaute at the Supplementary Site.","authors":"Kun Xi, Jinchu Liu, Wenzhuo Ma, Lizhe Zhu","doi":"10.1021/acs.biochem.5c00056","DOIUrl":"10.1021/acs.biochem.5c00056","url":null,"abstract":"Thermus thermophilus Argonaute (TtAgo) utilizes a guide DNA strand to cleave foreign DNA, defending the bacteria against invasive genetic elements and thus offering potential as a gene-editing tool. However, the underlying mechanism for target recognition remains underexplored. For example, the necessity of guide-target complementarity at the supplementary site (positions g13-16) for target cleavage has been debated for years. Here, using multiple transition pathways generated by atomistic molecular dynamics simulations, we identified three stages in this process: tail release, base pairing, and final refinement. The tail release leads to full exposure of the guide DNA (gDNA) to solvents, thereby positioning base-pairing between gDNA and target DNA (tDNA) as the principal force driving recognition. Consequently, all rate-determining steps are situated within the base-pairing stage. Detailed examination indicates that π-π stacking between the nucleobases, the extrusion of bases, and mismatches significantly influence these rate-limiting stages. Our results also suggest that base dislocations are less disruptive factors than π-π stacking for tDNA recognition in the supplementary site.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2181-2191"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Pharmacological Characterization of Dopamine Receptor DRD1 Variants and Exploration of Their Allosteric Activation. 多巴胺受体DRD1变异的药理学特征及其变构激活的探索。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-01 DOI: 10.1021/acs.biochem.4c00877

Chao Wu, Kexin Wang, Zhiyu Liu, Siyuan Shen, Zhiqian Yang, Zhenhua Shao, Wei Yan

{"title":"Pharmacological Characterization of Dopamine Receptor DRD1 Variants and Exploration of Their Allosteric Activation.","authors":"Chao Wu, Kexin Wang, Zhiyu Liu, Siyuan Shen, Zhiqian Yang, Zhenhua Shao, Wei Yan","doi":"10.1021/acs.biochem.4c00877","DOIUrl":"10.1021/acs.biochem.4c00877","url":null,"abstract":"G protein-coupled receptors (GPCRs) are major drug targets, yet genetic variations in these receptors can alter drug responses, leading to significant challenges in healthcare. Despite the prevalence of GPCR-targeting drugs, the effects of these genetic variations on receptor function remain underexplored. This study establishes a framework for allosterically rescuing loss-of-function (LoF) variants in GPCRs, using the dopamine receptor D1 (DRD1) as a model. We characterized 49 DRD1 variants from genetic databases and literature, finding that most variants exhibit reduced membrane expression. Structural analysis indicated that variants within the ligand-binding pocket or near critical activation motifs may impair ligand binding or hinder conformational changes during receptor activation, potentially disrupting orthosteric ligand induced signaling. We categorized the variants into three functional groups: those with enhanced G protein signaling, enhanced β-arrestin recruitment, or complete LoF. Among these, 16 variants disrupt G protein signaling, and 27 impair β-arrestin recruitment in HEK293 cells. Notably, defective G protein signaling caused by LoF variants such as T371.46K and L662.46F were effectively restored using allosteric modulators. These findings highlight the functional impact of DRD1 variants and demonstrate the therapeutic potential of relative selectivity of two signal pathways. This study advances precision medicine by offering strategies to restore receptor function and develop targeted therapies for GPCR-related disorders.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2200-2211"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Characterization of a Highly Solvent-Tolerant SGNH Hydrolase Superfamily Lipolytic Enzyme from Sphaerobacter thermophilus. 嗜热球杆菌高耐溶剂SGNH水解酶超家族脂肪酶的表征

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 DOI: 10.1021/acs.biochem.5c00057

Kelsey Minium, Zachary J Knepp, Morgan Sutton, Tabatha Falls, Sara Bobb, Connor McKeefery, Kailynn Smith, Kyle T Root

{"title":"Characterization of a Highly Solvent-Tolerant SGNH Hydrolase Superfamily Lipolytic Enzyme from Sphaerobacter thermophilus.","authors":"Kelsey Minium, Zachary J Knepp, Morgan Sutton, Tabatha Falls, Sara Bobb, Connor McKeefery, Kailynn Smith, Kyle T Root","doi":"10.1021/acs.biochem.5c00057","DOIUrl":"https://doi.org/10.1021/acs.biochem.5c00057","url":null,"abstract":"Thermophilic microbial lipases that retain activity under harsh conditions are a highly desirable tool for catalysis in numerous biosynthetic and biotechnological applications. In this study, a putative SGNH lipase gene, from Sphaerobacter thermophilus (StSGNH1), was overexpressed using a pMCSG7 plasmid in BL21(DE3) cells. The polyhistidine-tagged enzyme was expressed as inclusion bodies that were readily solubilized using Empigen BB detergent, and the protein was purified to homogeneity using immobilized metal affinity chromatography. The classification of StSGNH1 as a thermophilic and alkaliphilic lipase was supported by its ability to optimally catalyze the hydrolysis of medium-length p-nitrophenol esters at elevated temperature (55 °C) and pH (8-11). Evaluation of the StSGNH1 structure generated by AlphaFold indicated that the catalytic domain was composed of a three-layered α/β/α fold, and molecular docking studies yielded insight into which residues proximal to the active site assist in stabilizing the ligand-enzyme interaction and substrate selectivity. Notably, StSGNH1 was able to carry out ester hydrolysis in the presence of elevated concentrations of detergents, chaotropic reagents, and organic solvents, indicating that it would be suitable for employment in industrial reactions. Tryptophan fluorescence measurements in the presence of guanidine hydrochloride were employed to estimate the free energy of folding for StSGNH1 along a reversible folding pathway. The properties of StSGNH1 would be highly desirable for biotechnological applications.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":""},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144109050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Effect of Phosphoserine-Containing Membranes on Electrostatic Fields at the Protein-Protein Interface Measured through Vibrational Stark Effect Spectroscopy. 用振动斯塔克效应光谱测定含丝氨酸膜对蛋白-蛋白界面静电场的影响。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-09 DOI: 10.1021/acs.biochem.5c00028

Jackson C Fink, Lauren J Webb

{"title":"The Effect of Phosphoserine-Containing Membranes on Electrostatic Fields at the Protein-Protein Interface Measured through Vibrational Stark Effect Spectroscopy.","authors":"Jackson C Fink, Lauren J Webb","doi":"10.1021/acs.biochem.5c00028","DOIUrl":"10.1021/acs.biochem.5c00028","url":null,"abstract":"In the cell, Ras GTPases function as membrane-bound molecular switches for a variety of cell signaling pathways. Ras isoforms have long been of interest because of the connection between amino acid mutations and tumorigenesis. Much research focused on Ras has used truncated, solubilized constructs, which exclude the membrane-binding domain and therefore ignore the effects of membrane binding on Ras function. Since the membrane is a highly charged surface, it could have a significant impact on the electrostatic environment at or near the protein-protein interface. Here, we use a thiocyanate probe chemically inserted into the Ras-binding domain of RalGDS to investigate the effect of membrane binding at the Ras active site. Changes in the electric field caused by the membrane were measured by the probe as vibrational energy shifts in the infrared (IR) spectrum. For a selection of mutants which caused large shifts at this interface on the soluble H-Ras construct, binding to a 30% phosphatidylserine (PS)/70% phosphatidylcholine (PC) nanodisc caused reduced shifts compared to the solubilized counterparts. Additionally, the vibrational probe bonded to the wildtype (WT) Ras construct demonstrated a shift of 0.7 cm-1 as a PC nanodisc was doped from 0% to 30% PS, but mutations introduced to the Ras active site caused the probe to show no shift across these PS concentrations. These results indicate that the local membrane environment has an effect on the electrostatics at the Ras active site and needs to be considered when investigating the effect of oncogenic mutations on Ras function.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2280-2290"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143952193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Redox Homeostasis within the Drug-Resistant Malarial Parasite Digestive Vacuole. 耐药疟原虫消化液泡内的氧化还原稳态。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-01 DOI: 10.1021/acs.biochem.4c00750

Andreas Willems, Therese Oertel, Paul D Roepe

{"title":"Redox Homeostasis within the Drug-Resistant Malarial Parasite Digestive Vacuole.","authors":"Andreas Willems, Therese Oertel, Paul D Roepe","doi":"10.1021/acs.biochem.4c00750","DOIUrl":"10.1021/acs.biochem.4c00750","url":null,"abstract":"We have developed a cost-effective strategy for the complete synthesis of azetidinyl coumarin fluorophore derivatives that report changes in physiologic levels of glutathione (GSH), which includes a more cost- effective synthesis of the probe precursor hydroxyl derivative and its subsequent derivatization to promote subcellular localization. We functionalize coumarin derivatives with a cyano side chain similar to a previous strategy (Jiang X. et al., Nature Communications 2017, 8; 16087) and validate the 7-azetidinyl conformation as an explanation for enhanced GSH-dependent coumarin fluorescence. We couple the azetidinyl probe to different mass dextrans using either no linker or a 6C linker and also synthesize a morpholino derivative. We titrate the fluorescence of the different functionalized probes vs [GSH] in vitro. We load one dextran-conjugated probe within the digestive vacuole (DV) of live intraerythrocytic P. falciparum malarial parasites and also measure cytosolic localization of the morpholino probe. Using significantly improved single-cell photometry (SCP) methods, we show that the morpholino probe faithfully reports [GSH] from the live parasite cytosol, while the 70 kDa dextran-conjugated probe reports DV redox homeostasis for control chloroquine-sensitive (CQS) and artemisinin-sensitive (ARTS) transfectant parasites vs their genetically matched chloroquine-resistant (CQR)/artemisinin-sensitive (CQR/ARTS) and CQR artemisinin-resistant (CQR/ARTR) strains, respectively. We quantify rapid changes in DV redox homeostasis for these parasites ± drug pulses under live-cell perfusion conditions. The results are important for understanding the pharmacology of antimalarial drugs and the molecular mechanisms underlying CQR and ARTR phenomena.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2247-2261"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12096432/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143953400","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Identification and Functional Characterization of the Polymerizing Glycosyltransferase Required for the Transfer of d-Ribose to the d-GalfNAc Moiety of the Capsular Polysaccharide of Campylobacter jejuni. 空肠弯曲杆菌荚膜多糖d-核糖向d-GalfNAc部分转移所需的聚合糖基转移酶的鉴定和功能表征

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-01 DOI: 10.1021/acs.biochem.5c00052

Dao Feng Xiang, Tamari Narindoshvili, Frank M Raushel

{"title":"Identification and Functional Characterization of the Polymerizing Glycosyltransferase Required for the Transfer of d-Ribose to the d-GalfNAc Moiety of the Capsular Polysaccharide of Campylobacter jejuni.","authors":"Dao Feng Xiang, Tamari Narindoshvili, Frank M Raushel","doi":"10.1021/acs.biochem.5c00052","DOIUrl":"10.1021/acs.biochem.5c00052","url":null,"abstract":"Campylobacter jejuni is the leading cause of food poisoning in the United States. The exterior surface of this bacterium is coated with a capsular polysaccharide (CPS) that helps protect the organism from the host immune system. In the HS:2 serotype of strain C. jejuni NCTC 11168, the minimal repeating trisaccharide consist of d-ribose, N-acetyl-d-galactosamine (GalNAc) and the serinol amide of d-glucuronic acid. Here we demonstrate that the C-terminal domain of Cj1432 (residues 574-914) is responsible for the transfer of d-ribose-5-P from phosphoribosyl pyrophosphate (PRPP) to C5 of the d-GalfNAc moiety of the growing polysaccharide chain. In the next step the middle domain of Cj1432 (residues 357-573) catalyzes the hydrolysis of phosphate from this product. The N-terminal domain of Cj1432 (residues 1-356) catalyzes the transfer of d-GlcA from UDP-d-GlcA to C2 of the d-ribose moiety and thus Cj1432 catalyzes three consecutive reactions during the biosynthesis of the capsular polysaccharide of C. jejuni. We have previously shown that the remaining three reactions required for the polymerization of the CPS are catalyzed by the bifunctional enzyme Cj1438 and Cj1435. We have now demonstrated that the minimal repeating trisaccharide of the CPS of C. jejuni NCTC 11168 requires six enzyme-catalyzed reactions with six intermediate structures. This accomplishment will now enable the large-scale cell-free enzyme-catalyzed synthesis of well-defined oligomers of the CPS that can potentially be used in the production of glycoconjugate vaccines for the prevention of infections by C. jejuni.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2226-2236"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12096443/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955680","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

An Alkaliphilic Chitinase Unveils Environment-Dependent Variation in the Canonical Catalytic Machinery of Family-18 Glycoside Hydrolases. 一种亲碱几丁质酶揭示了18家族糖苷水解酶典型催化机制的环境依赖性变异。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-20 Epub Date: 2025-05-02 DOI: 10.1021/acs.biochem.5c00082

Jogi Madhuprakash, Bjørn Dalhus, Bastien Bissaro, Lal Duhsaki, Gustav Vaaje-Kolstad, Morten Sørlie, Åsmund K Røhr, Vincent G H Eijsink

{"title":"An Alkaliphilic Chitinase Unveils Environment-Dependent Variation in the Canonical Catalytic Machinery of Family-18 Glycoside Hydrolases.","authors":"Jogi Madhuprakash, Bjørn Dalhus, Bastien Bissaro, Lal Duhsaki, Gustav Vaaje-Kolstad, Morten Sørlie, Åsmund K Røhr, Vincent G H Eijsink","doi":"10.1021/acs.biochem.5c00082","DOIUrl":"10.1021/acs.biochem.5c00082","url":null,"abstract":"Chitinases belonging to glycoside hydrolase family-18 (GH18) employ substrate-assisted catalysis and typically have neutral/acidic pH-optima. We describe the structural and functional analysis of CaChiA, a chitinase from the anaerobic alkaliphilic bacterium Chitinivibrio alkaliphilus with an alkaline pH optimum (8.8) and unique active site features, including a noncanonical catalytic HxxExDxE motif, which is DxxDxDxE in other chitinases. Propka calculations indicated a significantly higher pKa for the catalytic acid/base, Glu148, in CaGH18, compared to other GH18 enzymes, aligning with its alkaline pH optimum. Both Propka calculations and functional studies of enzyme variants with mutations in the catalytic center suggested that not the change in the catalytic motif, but rather a unique glutamine, Gln57, modulating the properties of this motif, enables activity at alkaline pH. Further characterization of CaChiA unveiled additional peculiar enzyme properties, such as a unique ability to convert chitin to chitotriose. Thus, CaChiA adds novel catalytic capabilities to the widespread family of GH18 chitinases, made possible by adaptation of an intricate catalytic center.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":"2291-2305"},"PeriodicalIF":2.9,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143954047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Emergent and Convergent Features in the Laboratory Evolution of Polymerase Ribozymes. 聚合酶核酶实验室进化中的突现与趋同特征。

IF 2.9 3区生物学

Biochemistry Biochemistry Pub Date : 2025-05-19 DOI: 10.1021/acs.biochem.5c00160

David P Horning

{"title":"Emergent and Convergent Features in the Laboratory Evolution of Polymerase Ribozymes.","authors":"David P Horning","doi":"10.1021/acs.biochem.5c00160","DOIUrl":"https://doi.org/10.1021/acs.biochem.5c00160","url":null,"abstract":"In modern biology, molecular heredity is established by polymerase proteins that copy genetic information encoded in the sequence of nucleic acids. Prior to the emergence of coded protein synthesis, this role may have been filled by RNA polymerase ribozymes. Although such enzymes can no longer be found in extant life, ribozymes first evolved from random sequence populations have been progressively engineered in the laboratory to function as general RNA-dependent RNA polymerases. Polymerase ribozymes discovered in the past ten years can catalyze hundreds of sequential RNA synthesis reactions, match the complexity and catalytic sophistication of biological RNA enzymes, and employ many of the same strategies used by polymerase proteins to copy nucleic acids. This review describes the approaches to directed in vitro evolution that have led to the discovery of RNA enzymes that copy RNA molecules processively and accurately, and surveys how laboratory evolution has shaped biochemical and structural adaptations in these enzymes. The review then considers the challenges and opportunities that remain in the effort to propagate and evolve RNA genes with RNA catalysts alone.","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":""},"PeriodicalIF":2.9,"publicationDate":"2025-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144100967","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0