{"title":"Evolutionary assembly of the flagellar cage: repurposing a Type IV pili subcomplex.","authors":"Xueyin Feng, Yingyi Huang, Yanran Liu, Beile Gao","doi":"10.1016/j.tibs.2026.08.014","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.014","url":null,"abstract":"<p><p>Flagella, the major motility organelles in bacteria, display great diversity and complexity in their motor structures. Aside from the classical model with a simple motor, the functions of the components of complex motors are beginning to be explored. Recently, flagellar motors in Campylobacterota were found to have homologs of Type IV pili (T4P). Here, we review how these homologs form a peripheral cage structure in the motor, enclosing stator units and influencing motor assembly and function. We highlight structural features, including conformational variability and a proposed two-step assembly process, and synthesize evidence for their possible origin via exaptation of T4P components in the common ancestor of Campylobacterota. This work focuses on the evolution, structure, and functional integration of a co-opted subcomplex, shedding light on the re-engineering of nanomachines.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149023516","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Cable bacteria use extracellular electron transfer.","authors":"Nicole M J Geerlings","doi":"10.1016/j.tibs.2026.08.007","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.007","url":null,"abstract":"<p><p>Recent work by Aiyer and colleagues demonstrates that cable bacteria can conserve energy and grow under anoxic conditions by transferring electrons to electrodes via extracellular electron transfer. This transfer is both direct and riboflavin-mediated. Two distinct outer cell-surface redox centers, likely outer-membrane cytochromes, are involved in the electron transfer.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148975299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"SNOR: a path for ribosome recovery after hibernation.","authors":"Brenna A Saladin, Jailson Brito Querido","doi":"10.1016/j.tibs.2026.08.009","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.009","url":null,"abstract":"<p><p>Cellular dormancy requires ribosomes to be reversibly silenced yet preserved. Gluc et al. identify Shwachman-Bodian-Diamond syndrome domain-containing hibernation factor (SNOR), a fission yeast hibernation factor induced specifically by perturbed glucose homeostasis. Rather than driving translational shutdown, SNOR maintains dormant ribosomes in a state competent for rapid reactivation.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148966175","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Autophagy reshapes plant hormone signaling.","authors":"Yuping Li, Ying Wang, Chao Yang","doi":"10.1016/j.tibs.2026.08.013","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.013","url":null,"abstract":"<p><p>Recent breakthroughs in autophagy highlight it as a vital pathway, beyond the ubiquitin-proteasome system and the endosomal pathway, in plant hormone signal transduction, where it selectively targets key transcription factors for vacuolar turnover. Here, we review and discuss the emerging interplay between autophagy and hormone signaling pathways.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148943865","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Pyruvylation expands the redox repertoire of lysine acylation.","authors":"Jun Seo Park, Sung Joong Lee","doi":"10.1016/j.tibs.2026.08.008","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.008","url":null,"abstract":"<p><p>Song et al. establish lysine pyruvylation (Kpy) as an acylation response to glycolytic flux and pyruvate availability, detect pyruvyl-CoA, implicate histone acetyltransferase 1 and p300 as writers and sirtuin 3 as an eraser, and link promoter-associated histone Kpy to transcriptional regulation, defining a distinct C3 acylation alongside lactylation at the redox-coupled pyruvate-lactate node.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148904765","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yuan-Fei Zhou, Ling Zhang, D M Nirosh Udayanga, Nima Sharifi, Zhipeng A Wang
{"title":"A framework for understanding post-translational modifications of metabolic origin.","authors":"Yuan-Fei Zhou, Ling Zhang, D M Nirosh Udayanga, Nima Sharifi, Zhipeng A Wang","doi":"10.1016/j.tibs.2026.08.006","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.006","url":null,"abstract":"<p><p>Metabolites, beyond their canonical roles in energy production and biosynthesis, also serve as precursors for a diverse array of post-translational modifications (PTMs). The functional significance of PTMs in physiology and disease has attracted increasing attention, and the landscape of metabolite-mediated PTMs has expanded markedly in recent years. In this review, we summarize recently identified metabolite-mediated PTMs categorized by their diverse metabolic origins, along with their proteomic discoveries, regulations, and functions. We further highlight the utility of chemical proteomics in uncovering previously unrecognized PTMs and discuss current challenges in studying PTMs. Together, these advances enhance our understanding of the connection between metabolism and PTMs.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890499","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ugne Gaizauskaite, Inga Songailiene, Giedrius Sasnauskas, Virginijus Siksnys
{"title":"Building CRISPR immunity: evolution and mechanisms of spacer acquisition.","authors":"Ugne Gaizauskaite, Inga Songailiene, Giedrius Sasnauskas, Virginijus Siksnys","doi":"10.1016/j.tibs.2026.08.004","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.08.004","url":null,"abstract":"<p><p>CRISPR-Cas systems in prokaryotes serve as adaptive immune systems that neutralize phage infections through RNA-guided nucleases. Immunization is achieved during the adaptation stage through Cas1-Cas2 integrase-mediated insertion of short foreign DNA snippets, termed spacers, into a CRISPR array in the host genome. This review examines the evolutionary origins of Cas1-Cas2 and the mechanisms of spacer acquisition in DNA-targeting CRISPR-Cas systems. Particular emphasis is placed on the recently characterized effector-assisted adaptation pathways, in which CRISPR effector proteins, such as Cascade and Cas9, typically involved in target interference, are repurposed for prespacer capture and integration into a CRISPR array.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148885788","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The diversity of terminal electron acceptors across eukaryotes.","authors":"Ayush D Midha, Isha H Jain","doi":"10.1016/j.tibs.2026.07.009","DOIUrl":"10.1016/j.tibs.2026.07.009","url":null,"abstract":"<p><p>The flow of electrons is essential for life. To sustain metabolic flux, organisms efficiently transfer electrons to terminal electron acceptors, which range from inorganic nutrients to intracellularly derived organic metabolites. While the rise of atmospheric oxygen favored the expansion of high-yield aerobic respiration, the diversity of anaerobic electron acceptors remains important for organismal and ecological health, particularly in response to fluctuations in nutrient availability. This review summarizes respiratory and fermentative electron acceptors across eukaryotes, focusing on the evolution of anaerobic pathways. We highlight how ancient metabolic strategies have been conserved and modified to support organisms' adaptation to diverse environmental niches and to sustain biological resilience.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13591958/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148885830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A metabolon channels nicotine biosynthesis","authors":"Hao Zhang, Benke Hong","doi":"10.1016/j.tibs.2026.06.003","DOIUrl":"10.1016/j.tibs.2026.06.003","url":null,"abstract":"<div><div>A recent study by <span><span>Chang <em>et al.</em></span><svg><path></path></svg></span> uncovers a series of cryptic glycosylated intermediates and previously elusive enzymes that complete the nicotine biosynthesis. They demonstrate that nicotine biosynthetic enzymes and a transporter assemble into a vacuolar membrane metabolon that enables substrate channeling, enhances pathway efficiency, and promotes nicotine accumulation.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 9","pages":"Pages 859-861"},"PeriodicalIF":14.4,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148374122","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Modification and aminoacylation of human mitochondrial tRNAs","authors":"Shi-Ying Yao, Meng Wang, Fan-Yan Wei, Xiao-Long Zhou","doi":"10.1016/j.tibs.2026.06.009","DOIUrl":"10.1016/j.tibs.2026.06.009","url":null,"abstract":"<div><div>Mitochondrial tRNAs (mt-tRNAs) are central to energy production by translating essential oxidative phosphorylation subunits. Following transcription, mt-tRNAs undergo diverse processing steps, post-transcriptional modifications, and aminoacylation, which are critical for their functions. In this article, we review how human mt-tRNA-modifying enzymes deposit various post-transcriptional modifications onto mt-tRNAs, encompassing both well-characterized and less-understood marks. We also summarize the principles, peculiarities, and critical roles of mt-tRNA charging and proofreading, and highlight recently uncovered noncanonical functions of mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs). Collectively, these recent findings demonstrate the dynamic regulatory mechanisms of mt-tRNA modification and aminoacylation, the extensive involvement of mt-aaRSs in cellular metabolic pathways, and the promising potential of targeting these enzymes in therapeutics.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 9","pages":"Pages 937-954"},"PeriodicalIF":14.4,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148454222","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}