{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T21:44:16Z","timestamp":1792100656490,"version":"4.4.0"},"reference-count":88,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T00:00:00Z","timestamp":1785801600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100031022","name":"Center for Cancer Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100031022","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Reports"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.celrep.2026.117887","type":"journal-article","created":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T12:04:45Z","timestamp":1787400285000},"page":"117887","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["16S ribosomal RNA modification drives transcript-specific translation efficiency"],"prefix":"10.1016","volume":"45","author":[{"given":"Zachory M.","family":"Park","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina R.","family":"Savage","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda R.","family":"Decker-Farrell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chin-Hsien","family":"Tai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tapan K.","family":"Maity","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weiming","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lisa M.","family":"Jenkins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2335-3568","authenticated-orcid":false,"given":"Kumaran S.","family":"Ramamurthi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.celrep.2026.117887_bib1","doi-asserted-by":"crossref","first-page":"6486","DOI":"10.1016\/j.cell.2024.10.035","article-title":"The ribosome comes to life","volume":"187","author":"Noller","year":"2024","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib2","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2023.0393","article-title":"Ribosomes: from conserved origin to functional\/medical mobility and heterogeneity","volume":"380","author":"Rivalta","year":"2025","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1016\/j.celrep.2026.117887_bib3","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0092-8674(00)00084-2","article-title":"Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution","volume":"102","author":"Schluenzen","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib4","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/35030006","article-title":"Structure of the 30S ribosomal subunit","volume":"407","author":"Wimberly","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2026.117887_bib5","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1126\/science.1060089","article-title":"Crystal structure of the ribosome at 5.5 A resolution","volume":"292","author":"Yusupov","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.celrep.2026.117887_bib6","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00058-25","article-title":"Bacterial ribosome heterogeneity facilitates rapid response to stress","volume":"207","author":"Shen","year":"2025","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib7","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1126\/science.abb0993","article-title":"A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress","volume":"370","author":"Lamper","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.celrep.2026.117887_bib8","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1016\/j.cell.2017.05.022","article-title":"The Mammalian Ribo-interactome Reveals Ribosome Functional Diversity and Heterogeneity","volume":"169","author":"Simsek","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib9","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molcel.2017.05.021","article-title":"Heterogeneous Ribosomes Preferentially Translate Distinct Subpools of mRNAs Genome-wide","volume":"67","author":"Shi","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib10","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.celrep.2018.08.093","article-title":"Endogenous rRNA Sequence Variation Can Regulate Stress Response Gene Expression and Phenotype","volume":"25","author":"Kurylo","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.celrep.2026.117887_bib11","doi-asserted-by":"crossref","first-page":"19487","DOI":"10.1073\/pnas.2009607117","article-title":"Selective translation by alternative bacterial ribosomes","volume":"117","author":"Chen","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008837","article-title":"Control of mRNA translation by dynamic ribosome modification","volume":"16","author":"Grenga","year":"2020","journal-title":"PLoS Genet."},{"key":"10.1016\/j.celrep.2026.117887_bib13","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.biochi.2014.11.019","article-title":"What do we know about ribosomal RNA methylation in Escherichia coli?","volume":"117","author":"Sergeeva","year":"2015","journal-title":"Biochimie"},{"key":"10.1016\/j.celrep.2026.117887_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/genes12081125","article-title":"RNA Modifications in Pathogenic Bacteria: Impact on Host Adaptation and Virulence","volume":"12","author":"Antoine","year":"2021","journal-title":"Genes"},{"key":"10.1016\/j.celrep.2026.117887_bib15","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1261\/rna.1371409","article-title":"Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria","volume":"15","author":"Giessing","year":"2009","journal-title":"RNA"},{"key":"10.1016\/j.celrep.2026.117887_bib16","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1011968","article-title":"Epitranscriptional m6A modification of rRNA negatively impacts translation and host colonization in Staphylococcus aureus","volume":"20","author":"Shields","year":"2024","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.celrep.2026.117887_bib17","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1038\/nsmb.1408","article-title":"A conserved rRNA methyltransferase regulates ribosome biogenesis","volume":"15","author":"Xu","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib18","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1107\/S2053230X14016999","article-title":"Purification, crystallization and preliminary crystallographic analysis of the 16S rRNA methyltransferase RsmI from Escherichia coli","volume":"70","author":"Zhao","year":"2014","journal-title":"Acta Crystallogr. F Struct. Biol. Commun."},{"key":"10.1016\/j.celrep.2026.117887_bib19","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.jsb.2012.04.011","article-title":"Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA","volume":"179","author":"Wei","year":"2012","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib20","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1093\/nar\/gkp1073","article-title":"Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA","volume":"38","author":"Kimura","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib21","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1038\/s41564-022-01257-y","article-title":"Ancient origin and constrained evolution of the division and cell wall gene cluster in Bacteria","volume":"7","author":"Megrian","year":"2022","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib22","doi-asserted-by":"crossref","first-page":"11203","DOI":"10.1093\/nar\/gkae626","article-title":"Complete list of canonical post-transcriptional modifications in the Bacillus subtilis ribosome and their link to RbgA driven large subunit assembly","volume":"52","author":"Popova","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib23","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2523453123","article-title":"Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI","volume":"123","author":"Barmada","year":"2026","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib24","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1128\/JB.01370-13","article-title":"The highly conserved MraZ protein is a transcriptional regulator in Escherichia coli","volume":"196","author":"Eraso","year":"2014","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib25","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00243-22","article-title":"MraZ Transcriptionally Controls the Critical Level of FtsL Required for Focusing Z-Rings and Kickstarting Septation in Bacillus subtilis","volume":"204","author":"White","year":"2022","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib26","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.3389\/fmicb.2019.02520","article-title":"Beyond a Ribosomal RNA Methyltransferase, the Wider Role of MraW in DNA Methylation, Motility and Colonization in Escherichia coli O157:H7","volume":"10","author":"Xu","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib27","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1111\/febs.13302","article-title":"Ribosomal RNA methyltransferases contribute to Staphylococcus aureus virulence","volume":"282","author":"Kyuma","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.celrep.2026.117887_bib28","doi-asserted-by":"crossref","first-page":"2058","DOI":"10.1021\/ja412084b","article-title":"Quantitative analysis of rRNA modifications using stable isotope labeling and mass spectrometry","volume":"136","author":"Popova","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.celrep.2026.117887_bib29","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/0092-8674(81)90164-1","article-title":"Cascades of Sigma factors","volume":"25","author":"Losick","year":"1981","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib30","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/0022-2836(90)90227-D","article-title":"Cascade regulation of spore coat gene expression in Bacillus subtilis","volume":"212","author":"Zheng","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib31","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00210-24","article-title":"A novel regulation on the developmental checkpoint protein Sda that controls sporulation and biofilm formation in Bacillus subtilis","volume":"207","author":"He","year":"2025","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib32","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00370-22","article-title":"Elongation Factor P Is Important for Sporulation Initiation","volume":"205","author":"Feaga","year":"2023","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib33","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1011633","article-title":"YebC2 resolves ribosome stalling and increases fitness of cells lacking EF-P and the ABCF ATPase YfmR","volume":"21","author":"Hong","year":"2025","journal-title":"PLoS Genet."},{"key":"10.1016\/j.celrep.2026.117887_bib34","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2314437121","article-title":"YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P","volume":"121","author":"Hong","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib35","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkaf1420","article-title":"Constant trouble with prolines-navigating a global translation dilemma","volume":"54","author":"Lassak","year":"2026","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib36","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1111\/1758-2229.12130","article-title":"Spore formation in Bacillus subtilis","volume":"6","author":"Tan","year":"2014","journal-title":"Environ. Microbiol. Rep."},{"key":"10.1016\/j.celrep.2026.117887_bib37","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1111\/j.1574-6976.2011.00310.x","article-title":"Recent progress in Bacillus subtilis sporulation","volume":"36","author":"Higgins","year":"2012","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.celrep.2026.117887_bib38","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1146\/annurev-micro-090816-093558","article-title":"Germination of Spores of the Orders Bacillales and Clostridiales","volume":"71","author":"Setlow","year":"2017","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib39","doi-asserted-by":"crossref","DOI":"10.1128\/mmbr.00080-22","article-title":"New Thoughts on an Old Topic: Secrets of Bacterial Spore Resistance Slowly Being Revealed","volume":"87","author":"Setlow","year":"2023","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.celrep.2026.117887_bib40","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.TBS-0023-2016","article-title":"The Spore Coat","volume":"4","author":"Driks","year":"2016","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.celrep.2026.117887_bib41","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1128\/jb.174.2.575-585.1992","article-title":"Characterization of spoIVA, a sporulation gene involved in coat morphogenesis in Bacillus subtilis","volume":"174","author":"Roels","year":"1992","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib42","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.molcel.2008.05.030","article-title":"ATP-driven self-assembly of a morphogenetic protein in Bacillus subtilis","volume":"31","author":"Ramamurthi","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib43","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.65845","article-title":"Reformulation of an extant ATPase active site to mimic ancestral GTPase activity reveals a nucleotide base requirement for function","volume":"10","author":"Updegrove","year":"2021","journal-title":"eLife"},{"key":"10.1016\/j.celrep.2026.117887_bib44","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1111\/1574-6968.12452","article-title":"An autoinhibitory conformation of the Bacillus subtilis spore coat protein SpoIVA prevents its premature ATP-independent aggregation","volume":"358","author":"Castaing","year":"2014","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.celrep.2026.117887_bib45","doi-asserted-by":"crossref","first-page":"E151","DOI":"10.1073\/pnas.1210554110","article-title":"ATP hydrolysis by a domain related to translation factor GTPases drives polymerization of a static bacterial morphogenetic protein","volume":"110","author":"Castaing","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib46","doi-asserted-by":"crossref","first-page":"21789","DOI":"10.1073\/pnas.1907397116","article-title":"A 2-dimensional ratchet model describes assembly initiation of a specialized bacterial cell surface","volume":"116","author":"Peluso","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib47","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1146\/annurev-micro-041522-103140","article-title":"To Sporulate or Not to Sporulate: Developmental Checkpoints Monitoring Bacillus subtilis Sporulation","volume":"79","author":"Park","year":"2025","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib48","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.devcel.2021.12.021","article-title":"Bacterial developmental checkpoint that directly monitors cell surface morphogenesis","volume":"57","author":"Delerue","year":"2022","journal-title":"Dev. Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib49","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2414737121","article-title":"Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function","volume":"121","author":"Delerue","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2026.117887_bib50","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.devcel.2015.08.009","article-title":"A Quality-Control Mechanism Removes Unfit Cells from a Population of Sporulating Bacteria","volume":"34","author":"Tan","year":"2015","journal-title":"Dev. Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib51","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.tim.2017.03.005","article-title":"Cell Death Pathway That Monitors Spore Morphogenesis","volume":"25","author":"Decker","year":"2017","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib52","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1128\/JB.183.5.1645-1654.2001","article-title":"Amino acids in the Bacillus subtilis morphogenetic protein SpoIVA with roles in spore coat and cortex formation","volume":"183","author":"Catalano","year":"2001","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib53","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1126\/science.270.5236.641","article-title":"Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division","volume":"270","author":"Duncan","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.celrep.2026.117887_bib54","doi-asserted-by":"crossref","first-page":"3437","DOI":"10.1002\/pmic.200400997","article-title":"Identification of the degradome of Isp-1, a major intracellular serine protease of Bacillus subtilis, by two-dimensional gel electrophoresis and matrix- assisted laser desorption\/ionization-time of flight analysis","volume":"4","author":"Lee","year":"2004","journal-title":"Proteomics"},{"key":"10.1016\/j.celrep.2026.117887_bib55","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1111\/j.1365-2958.2004.04023.x","article-title":"Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis","volume":"52","author":"Hamon","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib56","article-title":"Mapping the rRNA methylome reveals contributions of methyltransferases to ribosome function and antibiotic sensitivity","author":"Hibma","year":"2026","journal-title":"bioRxiv"},{"key":"10.1016\/j.celrep.2026.117887_bib57","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/s41586-020-2638-5","article-title":"Functionally uncoupled transcription-translation in Bacillus subtilis","volume":"585","author":"Johnson","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2026.117887_bib58","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1038\/s41586-024-08308-w","article-title":"Tracking transcription-translation coupling in real time","volume":"637","author":"Qureshi","year":"2025","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2026.117887_bib59","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1126\/science.169.3943.392","article-title":"Visualization of bacterial genes in action","volume":"169","author":"Miller","year":"1970","journal-title":"Science"},{"key":"10.1016\/j.celrep.2026.117887_bib60","article-title":"Cross-species phenotypic profiling uncovers functional determinants of bacterial cold shock adaptation","author":"Fan","year":"2025","journal-title":"bioRxiv"},{"key":"10.1016\/j.celrep.2026.117887_bib61","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/s41580-024-00748-6","article-title":"Identification of RNA structures and their roles in RNA functions","volume":"25","author":"Cao","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib62","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1080\/10409230590918702","article-title":"Bacterial small RNA regulators","volume":"40","author":"Majdalani","year":"2005","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib63","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2025.169059","article-title":"Bacterial Regulatory Circuits are Linked and Extended by Small RNAs","volume":"437","author":"Gottesman","year":"2025","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib64","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2025.169045","article-title":"Unexpected Richness of the Bacterial Small RNA World","volume":"437","author":"Storz","year":"2025","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib65","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1146\/annurev-micro-091014-104306","article-title":"Riboswitch-Mediated Gene Regulation: Novel RNA Architectures Dictate Gene Expression Responses","volume":"70","author":"Sherwood","year":"2016","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib66","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.tibs.2022.08.009","article-title":"Discovering riboswitches: the past and the future","volume":"48","author":"Kavita","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.celrep.2026.117887_bib67","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagrm.2022.194871","article-title":"RNA thermometers in bacteria: Role in thermoregulation","volume":"1865","author":"Sharma","year":"2022","journal-title":"Biochim. Biophys. Acta, Gene Regul. Mech."},{"key":"10.1016\/j.celrep.2026.117887_bib68","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.cell.2004.11.042","article-title":"mRNA helicase activity of the ribosome","volume":"120","author":"Takyar","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2026.117887_bib69","doi-asserted-by":"crossref","first-page":"3195","DOI":"10.1093\/nar\/gkaa129","article-title":"The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development","volume":"48","author":"Zou","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib70","doi-asserted-by":"crossref","first-page":"8505","DOI":"10.1074\/jbc.RA119.012127","article-title":"The human mitochondrial 12S rRNA m(4)C methyltransferase METTL15 is required for mitochondrial function","volume":"295","author":"Chen","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.celrep.2026.117887_bib71","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1111\/j.1365-2958.2012.08052.x","article-title":"Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis","volume":"84","author":"Ebmeier","year":"2012","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib72","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0147-619X(84)90061-1","article-title":"Construction of a cloning site near one end of Tn917 into which foreign DNA may be inserted without affecting transposition in Bacillus subtilis or expression of the transposon-borne erm gene","volume":"12","author":"Youngman","year":"1984","journal-title":"Plasmid"},{"key":"10.1016\/j.celrep.2026.117887_bib73","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1128\/JB.181.3.781-790.1999","article-title":"A four-dimensional view of assembly of a morphogenetic protein during sporulation in Bacillus subtilis","volume":"181","author":"Price","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.celrep.2026.117887_bib74","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1101\/gad.1078303","article-title":"The master regulator for entry into sporulation in Bacillus subtilis becomes a cell-specific transcription factor after asymmetric division","volume":"17","author":"Fujita","year":"2003","journal-title":"Genes Dev."},{"key":"10.1016\/j.celrep.2026.117887_bib75","first-page":"267","article-title":"Prediction of RNA secondary structure by energy minimization","volume":"25","author":"Zuker","year":"1994","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib76","doi-asserted-by":"crossref","first-page":"3406","DOI":"10.1093\/nar\/gkg595","article-title":"Mfold web server for nucleic acid folding and hybridization prediction","volume":"31","author":"Zuker","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib77","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1186\/1748-7188-6-26","article-title":"ViennaRNA Package 2.0","volume":"6","author":"Lorenz","year":"2011","journal-title":"Algorithms Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib78","doi-asserted-by":"crossref","first-page":"D864","DOI":"10.1093\/nar\/gkae957","article-title":"A new framework for SubtiWiki, the database for the model organism Bacillus subtilis","volume":"53","author":"Elfmann","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib79","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1101\/gr.266932.120","article-title":"Accessing NCBI data using the NCBI Sequence Viewer and Genome Data Viewer (GDV)","volume":"31","author":"Rangwala","year":"2021","journal-title":"Genome Res."},{"key":"10.1016\/j.celrep.2026.117887_bib80","doi-asserted-by":"crossref","first-page":"W521","DOI":"10.1093\/nar\/gkae241","article-title":"The EMBL-EBI Job Dispatcher sequence analysis tools framework in 2024","volume":"52","author":"Madeira","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2026.117887_bib81","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2--a multiple sequence alignment editor and analysis workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.celrep.2026.117887_bib82","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.cels.2016.12.013","article-title":"Construction and Analysis of Two Genome-Scale Deletion Libraries for Bacillus subtilis","volume":"4","author":"Koo","year":"2017","journal-title":"Cell Syst."},{"key":"10.1016\/j.celrep.2026.117887_bib83","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1111\/j.1365-2958.2006.05468.x","article-title":"Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis","volume":"62","author":"Ramamurthi","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2026.117887_bib84","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00257-11","article-title":"Cellular architecture mediates DivIVA ultrastructure and regulates min activity in Bacillus subtilis","volume":"2","author":"Eswaramoorthy","year":"2011","journal-title":"mBio"},{"key":"10.1016\/j.celrep.2026.117887_bib85","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/978-1-0716-3491-2_17","article-title":"Assembling the Bacillus subtilis Spore Coat Basement Layer on Spherical Supported Lipid Bilayers","volume":"2727","author":"Updegrove","year":"2024","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.celrep.2026.117887_bib86","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1042\/bj1130029","article-title":"Commitment to sporulation in Bacillus subtilis and its relationship to development of actinomycin resistance","volume":"113","author":"Sterlini","year":"1969","journal-title":"Biochem. J."},{"key":"10.1016\/j.celrep.2026.117887_bib87","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adq0791","article-title":"Altruistic feeding and cell-cell signaling during bacterial differentiation actively enhance phenotypic heterogeneity","volume":"10","author":"Updegrove","year":"2024","journal-title":"Sci. Adv."},{"key":"10.1016\/j.celrep.2026.117887_bib88","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1038\/s41467-024-55196-9","article-title":"Ribosomes translocation into the spore of Bacillus subtilis is highly organised and requires peptidoglycan rearrangements","volume":"16","author":"Iwa\u0144ska","year":"2025","journal-title":"Nat. Commun."}],"container-title":["Cell Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124726009654?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124726009654?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T20:46:36Z","timestamp":1792097196000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2211124726009654"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":88,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["S2211124726009654"],"URL":"https:\/\/doi.org\/10.1016\/j.celrep.2026.117887","relation":{},"ISSN":["2211-1247"],"issn-type":[{"value":"2211-1247","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"16S ribosomal RNA modification drives transcript-specific translation efficiency","name":"articletitle","label":"Article Title"},{"value":"Cell Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.celrep.2026.117887","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"117887"}}