Journal of Bacteriology最新文献

{"title":"Loss of LasR function leads to decreased repression of <i>Pseudomonas aeruginosa</i> PhoB activity at physiological phosphate concentrations.","authors":"Amy Conaway, Dallas L Mould, Igor Todorovic, Deborah A Hogan","doi":"10.1128/jb.00189-24","DOIUrl":"10.1128/jb.00189-24","url":null,"abstract":"<p><p>The <i>Pseudomonas aeruginosa</i> LasR transcription factor plays a role in quorum sensing (QS) across phylogenetically distinct lineages. However, isolates with loss-of-function mutations in <i>lasR</i> (LasR- strains) are commonly found in diverse settings, including infections where they are associated with worse clinical outcomes. In LasR- strains, the LasR-regulated transcription factor RhlR can also be stimulated by the activity of the two-component system PhoR-PhoB in low-inorganic phosphate (Pi) conditions. Here, we demonstrate a novel link between LasR and PhoB in which the absence of LasR increases PhoB activity at physiological Pi concentrations and increases the Pi concentration necessary for PhoB inhibition. PhoB activity was also less sensitive to repression by Pi in mutants lacking different QS regulators (RhlR and PqsR) and in mutants lacking genes required for QS-induced phenazine production, suggesting that decreased phenazine production is one reason for increased PhoB activity in LasR- strains. In addition, the CbrA-CbrB two-component system, which can be more active in LasR- strains, was necessary for increased PhoB activity in LasR- strains, and loss of the CbrA-CbrB-controlled translational repressor Crc was sufficient to activate PhoB in LasR+ <i>P. aeruginosa</i>. Phenazines and CbrA-CbrB affected PhoB activity independently. The ∆<i>lasR</i> mutant also had PhoB-dependent growth advantages in the Pi-deplete medium and increased virulence-associated gene expression at physiological Pi, in part through reactivation of QS. This work suggests PhoR-PhoB activity may contribute to the fitness and virulence of LasR- <i>P. aeruginosa</i> and subsequent clinical outcomes.IMPORTANCELoss-of-function mutations in the gene encoding the <i>Pseudomonas aeruginosa</i> quorum sensing (QS) regulator LasR occur frequently and are associated with worse clinical outcomes. We have found that LasR- <i>P. aeruginosa</i> have elevated PhoB activity at physiological concentrations of inorganic phosphate (Pi). PhoB activity promotes Pi acquisition as well as the expression of QS and virulence-associated genes. Previous work has shown that PhoB induces RhlR, another QS regulator, in a LasR- mutant in low-Pi conditions. Here, we demonstrate a novel relationship wherein LasR represses PhoB activity through the production of phenazines and Crc-mediated translational repression. This work suggests PhoB activity may contribute to the increased virulence of LasR- <i>P. aeruginosa</i>.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0018924"},"PeriodicalIF":2.7,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143991148","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}

{"title":"Calcium signaling controls early stage biofilm formation and dispersal in <i>Vibrio fischeri</i>.","authors":"Jeremy J Esin, Karen L Visick, Abby R Kroken","doi":"10.1128/jb.00077-25","DOIUrl":"https://doi.org/10.1128/jb.00077-25","url":null,"abstract":"<p><p>Bacterial dispersal from a biofilm is presently the least-studied step of the biofilm life cycle. The symbiotic bacterial species <i>Vibrio fischeri</i> is a model organism for studying biofilms relevant to a eukaryotic host; however, methodology is lacking to readily study the dispersal of this microbe from biofilms formed in the lab. Here, we adapted a time-lapse assay to visualize biofilm dispersal by <i>V. fischeri</i>. We observed biofilm formation and dispersal for multiple <i>V. fischeri</i> isolates, which displayed a variety of biofilm architecture phenotypes and dispersal dynamics. We then investigated <i>V. fischeri</i> strain ES114 using genetic tools and mutants available for this strain. ES114 exhibited calcium-dependent biofilm formation followed by a rapid (less than 10 min) coordinated dispersal event that occurred approximately 5 h from the experimental start. Biofilm dispersal was largely independent of the dispersal-promoting protease encoded by <i>lapG</i>. Although we found no role under our conditions for either biofilm formation or dispersal for several other factors including polysaccharides and autoinducers, we determined that biofilm formation was enhanced, and dispersal was delayed, with increased concentrations of calcium. Furthermore, biofilm formation depended on the calcium-responsive diguanylate cyclase (DGC) CasA, and dispersal could be modulated by overexpressing CasA. Our work has thus developed a new tool for the <i>V. fischeri</i> field and uncovered a key role for calcium signaling and c-di-GMP in early biofilm formation and dispersal in <i>V. fischeri</i>.</p><p><strong>Importance: </strong>Biofilm formation and dispersal are critical steps in both symbiotic and pathogenic colonization. Relative to biofilm formation, the process of dispersal in the model symbiont <i>Vibrio fischeri</i>, and other bacteria, is understudied. Here, we adapted an imaging assay to study early biofilm formation and the dispersal process in <i>V. fischeri</i>. We demonstrated that our assay can quantify biofilm formation and dispersal over time, can reveal phenotypic differences in diverse natural wild-type isolates, and is sensitive enough to investigate the impact of environmental factors. Our data confirm that calcium is a potent biofilm formation signal and identify the diguanylate cyclase CasA as a key regulator. This work leads the way for more in-depth research about unknown mechanisms of biofilm dispersal.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0007725"},"PeriodicalIF":2.7,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143981983","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}

{"title":"<i>Haloferax volcanii</i>: a versatile model for studying archaeal biology.","authors":"Mechthild Pohlschroder, Stefan Schulze, Friedhelm Pfeiffer, Yirui Hong","doi":"10.1128/jb.00062-25","DOIUrl":"https://doi.org/10.1128/jb.00062-25","url":null,"abstract":"<p><p>Archaea, once thought limited to extreme environments, are now recognized as ubiquitous and fundamental players in global ecosystems. While morphologically similar to bacteria, they are a distinct domain of life and are evolutionarily closer to eukaryotes. The development of model archaeal systems has facilitated studies that have underscored unique physiological, biochemical, and genetic characteristics of archaea. <i>Haloferax volcanii</i> stands out as a model archaeon due to its ease of culturing, ability to grow on defined media, amenability to genetic and biochemical methods, as well as the support from a highly collaborative community. This haloarchaeon has been instrumental in exploring diverse aspects of archaeal biology, ranging from polyploidy, replication origins, and post-translational modifications to cell surface biogenesis, metabolism, and adaptation to high-salt environments. The extensive use of <i>Hfx. volcanii</i> further catalyzed the development of new technologies and databases, facilitating discovery-driven research that offers significant implications for biotechnology, biomedicine, and core biological questions.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0006225"},"PeriodicalIF":2.7,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143972476","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}

{"title":"CRISPRi-mediated repression of three <i>cI</i> repressors induces the expression of three related <i>Neisseria gonorrhoeae</i> bacteriophages.","authors":"Wendy E Geslewitz, H Steven Seifert","doi":"10.1128/jb.00049-25","DOIUrl":"https://doi.org/10.1128/jb.00049-25","url":null,"abstract":"<p><p>The <i>Neisseria gonorrhoeae</i> FA1090 isolate encodes nine prophage islands (Ngoɸ1-9). Ngoɸ1-3 contain genes consistent with a <i>Siphoviridae</i>-dsDNA bacteriophage (phage). Saturating transposon-sequencing screens using two different <i>N. gonorrhoeae</i> isolates predicted that multiple prophage genes were essential, including three putative transcriptional repressors: <i>ngo0479</i> (present in Ngoɸ1), <i>ngo1116</i> (present in Ngoɸ2), and <i>ngo1630</i> (present in Ngoɸ3). All three genes display homology to the Lambda phage <i>cI</i>, a regulator important for maintaining the lysogenic state and inhibiting lytic induction, but these proteins are not close paralogs. Using a <i>Neisseria lactamica</i>-derived Type I-C CRISPR-interference system, we show that these <i>cI</i> orthologs are essential, as the knockdown of each gene results in bacterial death. We determined that the repression of the three <i>cI</i> orthologs resulted in the significant induction of phage gene expression. Finally, we detected <i>Siphoviridae</i>-like phage particles released from <i>N. gonorrhoeae</i> following repression of <i>ngo0479</i>, <i>ngo1116</i>, or <i>ngo1630</i>. We hypothesize that these <i>cI</i> orthologs are critical for preventing phage lytic infection and cell death and allow <i>N. gonorrhoeae</i> to benefit from the carriage and expression of prophage genes.IMPORTANCEBacteriophage, or phage, are bacteria-infecting viruses and are the most abundant natural entities in the world. Here, we report that <i>Neisseria gonorrhoeae</i>'s three most complete double-stranded DNA prophage islands each encode essential and related transcriptional repressors. CRISPRi-mediated repression of these transcriptional repressors leads to a significant increase in prophage gene expression and phage induction. This study marks an important initial step in studying the interaction between <i>N. gonorrhoeae</i> and its resident phage.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0004925"},"PeriodicalIF":2.7,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143991585","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}

{"title":"Exploration and analytical techniques for membrane curvature-sensing proteins in bacteria.","authors":"Takumi Komikawa, Mina Okochi, Masayoshi Tanaka","doi":"10.1128/jb.00482-24","DOIUrl":"10.1128/jb.00482-24","url":null,"abstract":"<p><p>The mechanism by which cells regulate protein localization is an important topic in the field of bacterial biology. In certain instances, the morphology of the biological membrane has been demonstrated to function as a spatial cue for the subcellular localization of proteins. These proteins are capable of sensing membrane curvature and are involved in a number of physiological functions such as cytokinesis and the formation of membrane-bound organelles. This review presents recent advances in the <i>in vitro</i> evaluation of curvature-sensing properties using artificially controlled membranes and purified proteins, as well as microscopic live cell assays. However, these evaluation methodologies often require sophisticated experiments, and the number of identified curvature sensors remains limited. Thus, we present a comprehensive exploration of recently reported curvature-sensing proteins. Subsequently, we summarize the known curvature-sensing proteins in bacteria, in conjunction with the analytical methodologies employed in this field. Finally, future prospects and further requirements in the study of curvature-sensing proteins are discussed.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0048224"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004969/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143709843","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}

{"title":"<i>Burkholderia cenocepacia</i>-mediated inhibition of <i>Staphylococcus aureus</i> growth and biofilm formation.","authors":"Tiffany J Brandt, Hayden Skaggs, Thomas Hundley, Deborah R Yoder-Himes","doi":"10.1128/jb.00116-23","DOIUrl":"10.1128/jb.00116-23","url":null,"abstract":"<p><p><i>Staphylococcus aureus</i> asymptomatically colonizes the nasal cavity and pharynx of up to 60% of the human population and, as an opportunistic pathogen, can breach its normal habitat, resulting in life-threatening infections. <i>S. aureus</i> infections are of additional concern for populations with impaired immune function such as those with cystic fibrosis (CF) or chronic granulomatous disease. Multi-drug resistance is increasingly common in <i>S. aureus</i> infections, creating an urgent need for new antimicrobials or compounds that improve efficacy of currently available antibiotics. <i>S. aureus</i> biofilms, such as those found in the lungs of people with CF and in soft tissue infections, are notoriously recalcitrant to antimicrobial treatment due to the characteristic metabolic differences associated with a sessile mode of growth. In this work, we show that another CF pathogen, <i>Burkholderia cenocepacia</i>, produces one or more secreted compounds that can prevent <i>S. aureus</i> biofilm formation and inhibit existing <i>S. aureus</i> biofilms. The <i>B. cenocepacia</i>-mediated antagonistic activity is restricted to <i>S. aureus</i> species and perhaps some other staphylococci; however, this inhibition does not necessarily extend to other Gram-positive species. This inhibitory activity is due to death of <i>S. aureus</i> through a contact-independent mechanism, potentially mediated through the siderophore pyochelin and perhaps additional compounds. This works paves the way to better understanding of interactions between these two bacterial pathogens.IMPORTANCE<i>Staphylococcus aureus</i> is a major nosocomial pathogen responsible for infecting thousands of people each year. Some strains are becoming increasingly resistant to antimicrobials, and consequently new treatments must be sought. This paper describes the characterization of one or more compounds capable of inhibiting <i>S. aureus</i> biofilm formation and may potentially lead to development of a new therapeutic.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0011623"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004965/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143709565","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}

{"title":"DNA repair is essential for <i>Vibrio cholerae</i> growth on thiosulfate-citrate-bile salts-sucrose (TCBS) medium.","authors":"Alex J Wessel, Drew T T Johnson, Christopher M Waters","doi":"10.1128/jb.00004-25","DOIUrl":"10.1128/jb.00004-25","url":null,"abstract":"<p><p>Thiosulfate-citrate-bile salts-sucrose (TCBS) agar is a selective and differential media for the enrichment of pathogenic <i>Vibrios</i>. We observed that an exonuclease VII (<i>exoVII</i>) mutant of <i>Vibrio cholerae</i> failed to grow on TCBS agar, suggesting that DNA repair mutant strains may be hampered for growth in this selective media. Examination of the selective components of TCBS revealed that bile acids were primarily responsible for the toxicity of the <i>exoVII</i> mutant. Suppressor mutations in DNA gyrase restored growth of the <i>exoVII</i> mutants on TCBS, suggesting that TCBS inhibits DNA gyrase similar to the antibiotic ciprofloxacin. To better understand what factors are important for <i>V. cholerae</i> to grow on TCBS, we generated a randomly barcoded TnSeq (RB-TnSeq) library in <i>V. cholerae</i> and have used it to uncover a range of DNA repair mutants that also fail to grow on TCBS agar. The results of this study suggest that TCBS agar causes DNA damage to <i>V. cholerae</i> similarly to the mechanism of action of fluoroquinolones, and overcoming this DNA damage is critical for <i>Vibrio</i> growth on this selective medium.IMPORTANCETCBS is often used to diagnose cholera infection. We found that many mutant <i>V. cholerae</i> strains are attenuated for growth on TCBS agar, meaning they could remain undetected using this culture-dependent method. Hypermutator strains with defects in DNA repair pathways might be especially inhibited by TCBS. In addition, <i>V. cholerae</i> grown successively on TCBS agar develops resistance to ciprofloxacin.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0000425"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004951/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143709751","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}

{"title":"Identification of EcpK, a bacterial tyrosine pseudokinase important for exopolysaccharide biosynthesis in <i>Myxococcus xanthus</i>.","authors":"Luca Blöcher, Johannes Schwabe, Timo Glatter, Lotte Søgaard-Andersen","doi":"10.1128/jb.00499-24","DOIUrl":"10.1128/jb.00499-24","url":null,"abstract":"<p><p>Bacteria synthesize chemically diverse capsular and secreted polysaccharides that function in many physiological processes and are widely used in industrial applications. In the ubiquitous Wzx/Wzy-dependent biosynthetic pathways for these polysaccharides, the polysaccharide co-polymerase (PCP) facilitates the polymerization of repeat units in the periplasm, and in Gram-negative bacteria, also polysaccharide translocation across the outer membrane. These PCPs belong to the PCP-2 family, are integral inner membrane proteins with extended periplasmic domains, and functionally depend on alternating between different oligomeric states. The oligomeric state is determined by a cognate cytoplasmic bacterial tyrosine kinase (BYK), which is either part of the PCP or a stand-alone protein. Interestingly, BYK-like proteins, which lack key catalytic residues and/or the phosphorylated Tyr residues, have been described. In <i>Myxococcus xanthu</i>s, the exopolysaccharide (EPS) is synthesized and exported <i>via</i> the Wzx/Wzy-dependent EPS pathway in which EpsV serves as the PCP. Here, we confirm that EpsV lacks the BYK domain. Using phylogenomics, experiments, and computational structural biology, we identify EcpK as important for EPS biosynthesis and show that it structurally resembles canonical BYKs but lacks residues important for catalysis and Tyr phosphorylation. Using proteomic analyses, two-hybrid assays, and structural modeling, we demonstrate that EcpK directly interacts with EpsV. Based on these findings, we suggest that EcpK is a BY pseudokinase and functions as a scaffold, which by direct protein-protein interactions, rather than by Tyr phosphorylation, facilitates EpsV function. EcpK and EpsV homologs are present in other bacteria, suggesting broad conservation of this mechanism and establishing a phosphorylation-independent PCP-2 subfamily.IMPORTANCEBacteria produce a variety of polysaccharides with important biological functions. In Wzx/Wzy-dependent pathways for the biosynthesis of secreted and capsular polysaccharides in Gram-negative bacteria, the polysaccharide co-polymerase (PCP) is a key protein that facilitates repeat unit polymerization and polysaccharide translocation across the outer membrane. PCP function depends on assembly/disassembly cycles that are determined by the phosphorylation/dephosphorylation cycles of an associated bacterial tyrosine kinase (BYK). Here, we identify the BY pseudokinase EcpK as essential for exopolysaccharide biosynthesis in <i>Myxococcus xanthus</i>. Based on experiments and computational structural biology, we suggest that EcpK is a scaffold protein, guiding the assembly/disassembly cycles of the partner PCP <i>via</i> binding/unbinding cycles independently of Tyr phosphorylation/dephosphorylation cycles. We suggest that this novel mechanism is broadly conserved.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0049924"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004946/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143604928","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}

{"title":"A geranylgeranyl reductase homolog required for cholesterol production in Myxococcota.","authors":"Alysha K Lee, Paula V Welander","doi":"10.1128/jb.00495-24","DOIUrl":"10.1128/jb.00495-24","url":null,"abstract":"<p><p>Myxococcota is a phylum of sterol-producing bacteria. They exhibit a clade depth for sterol biosynthesis unparalleled in the bacterial domain and produce sterols of a biosynthetic complexity that rivals eukaryotes. Additionally, the sterol biosynthesis pathways found in this phylum have been proposed as a potential source for sterol biosynthesis in the last eukaryotic common ancestor, lending evolutionary importance to our understanding of this pathway in Myxococcota. However, sterol production has only been characterized in a few species, and outstanding questions about the evolutionary history of this pathway remain. Here, we identify two myxobacteria, <i>Minicystis rosea</i> and <i>Sandaracinus amylolyticus</i>, capable of cholesterol biosynthesis. These two myxobacteria possess a cholesterol biosynthesis pathway that differs in both the ordering and enzymes involved in biosynthesis compared with <i>Enhygromyxa salina</i>, a myxobacterium previously demonstrated to produce cholesterol, as well as the canonical pathways found in eukaryotes. We characterize an alternative bacterial reductase responsible for performing C-24 reduction, further delineating bacterial cholesterol production from eukaryotes. Finally, we examine the distribution and phylogenetic relationships of sterol biosynthesis proteins across both cultured and uncultured Myxococcota species, providing evidence for multiple acquisition events and instances of both horizontal and vertical transfer at the family level. Altogether, this work further demonstrates the capacity of myxobacteria to synthesize eukaryotic sterols but with an underlying diversity in the biochemical reactions that govern sterol synthesis, suggesting a complex evolutionary history and refining our understanding of how myxobacterial cholesterol production relates to their eukaryotic counterparts.</p><p><strong>Importance: </strong>Sterols are essential and ubiquitous lipids in eukaryotes, but their significance in bacteria is less understood. Sterol production in Myxococcota, a phylum of developmentally complex predatory bacteria, has provided insight into novel sterol biochemistry and prompted discussion regarding the evolution of this pathway within both the eukaryotic and bacterial domains. Here, we characterize cholesterol biosynthesis in two myxobacteria, providing evidence for distinct pathway organization and identifying a unique protein responsible for C-24 reduction. We couple these results with the phylogenomic analysis of sterol biosynthesis within Myxococcota, revealing a complicated evolutionary history marked by vertical and horizontal transfer. This suggests a mosaic acquisition of this pathway in Myxococcota and highlights the complex role myxobacteria may have had in sterol transfer to eukaryotes.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0049524"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004948/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143604926","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}

{"title":"A call for the United States to continue investing in science.","authors":"Ira Blader, Felicia Goodrum, Michael J Imperiale, Arturo Casadevall, Cesar A Arias, Andreas Baumler, Carey-Ann D Burnham, Christina A Cuomo, Corrella S Detweiler, Graeme N Forrest, Jack A Gilbert, Susan Lovett, Stanley Maloy, Alexander McAdam, Irene Newton, Gemma Reguera, George A O'Toole, Patrick D Schloss, Ashley Shade, Marvin Whiteley","doi":"10.1128/jb.00072-25","DOIUrl":"10.1128/jb.00072-25","url":null,"abstract":"","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0007225"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12004941/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143515568","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}