microLifePub Date : 2025-11-19eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf032
Paul B Rainey, Puri López-García, Zeynep Ceren Karahan, Paul Williams, Stipan Jonjić, Kenneth N Timmis
{"title":"Editorial: society journals matter-supporting science through renewed commitment.","authors":"Paul B Rainey, Puri López-García, Zeynep Ceren Karahan, Paul Williams, Stipan Jonjić, Kenneth N Timmis","doi":"10.1093/femsml/uqaf032","DOIUrl":"10.1093/femsml/uqaf032","url":null,"abstract":"","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf032"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12641116/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145607838","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-11-07eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf035
Jing Yuan, Hans-Georg Koch, Bork A Berghoff
{"title":"Functional diversity and molecular interactions of small membrane proteins in bacteria.","authors":"Jing Yuan, Hans-Georg Koch, Bork A Berghoff","doi":"10.1093/femsml/uqaf035","DOIUrl":"https://doi.org/10.1093/femsml/uqaf035","url":null,"abstract":"<p><p>Bacteria constantly adapt to changing environmental conditions through diverse processes that involve numerous regulator and effector proteins. In this regard, small proteins play a significant role in promoting stress adaptation in bacteria. Although they were largely overlooked in early genome annotations, recent technological advances and a growing recognition of their significance have paved the way for the increasing identification and characterization of this intriguing class of proteins. Many small proteins contain a transmembrane domain and are integral to the cytoplasmic membrane. Others interact with and modulate membrane protein complexes. In this review, we focus on the current knowledge of these small membrane proteins, with an emphasis on their interactions, membrane insertion pathways, and toxicity.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf035"},"PeriodicalIF":0.0,"publicationDate":"2025-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12648545/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145643608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-23eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf034
Liz Maria Luke, Kai Papenfort
{"title":"One transcript, two functions: the emerging roles of dual-function RNAs.","authors":"Liz Maria Luke, Kai Papenfort","doi":"10.1093/femsml/uqaf034","DOIUrl":"10.1093/femsml/uqaf034","url":null,"abstract":"<p><p>Bacteria use small regulatory RNAs (sRNAs) and small proteins to change gene expression and modulate cellular processes in response to changing environmental conditions. In addition, several transcripts have been reported to combine base-pairing sRNA activities and coding capacity. These transcripts are known as dual-function RNAs. In some cases, the sRNA and the protein operate within the same pathway, while in other cases, they modulate separate processes in the cell. Thereby, dual-function RNAs enable bacteria to adjust their gene expression and physiology at multiple levels, which can have synergistic regulatory effects or help to synchronize the output of cellular pathways. In this review, we summarized the regulatory and physiological roles of dual-function RNAs in bacteria, including their roles in intercellular communication, virulence, stress response, and metabolism. In addition, we discuss open challenges and possible future applications for harnessing dual regulators for precise gene expression control in bacteria.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf034"},"PeriodicalIF":0.0,"publicationDate":"2025-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12612679/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145544243","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-22eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf033
Doron Naki, Uri Gophna
{"title":"Evolutionary insights into provirus-encoded CRISPR-Cas systems in halophilic archaea.","authors":"Doron Naki, Uri Gophna","doi":"10.1093/femsml/uqaf033","DOIUrl":"10.1093/femsml/uqaf033","url":null,"abstract":"<p><p>Prokaryotic microorganisms coexist with mobile genetic elements (MGEs), which can be both genetic threats and evolutionary catalysts. In <i>Haloferax lucentense</i>, a halophilic archaeon, we have recently identified an unusual genomic arrangement: a complete type I-B CRISPR-Cas system encoded on a megaplasmid and an incomplete type I-B system within an integrated provirus in the main chromosome. The provirus-encoded system lacks the adaptation genes (<i>cas1, cas2</i>, and <i>cas4</i>), suggesting its potential reliance on the megaplasmid-encoded CRISPR-Cas module for the acquisition of new spacers. This arrangement suggests a potential instance of \"adaptive outsourcing,\" where a provirus might leverage a co-resident MGE for a key function. Through comparative genomics, we show that similar proviral CRISPR-Cas systems are found in distantly related haloarchaea (e.g. <i>Natrinema</i> and <i>Halobacterium</i>), indicating probable virus-mediated horizontal transfer and suggesting they may function as mobile defense modules. Phylogenetic analysis highlights distinct evolutionary origins of the two systems: the plasmid system clusters with other <i>Haloferax</i> CRISPR-Cas systems, while the proviral system clusters with those from other genera, consistent with horizontal acquisition. Interestingly, spacer analysis reveals that the proviral systems predominantly target viral sequences, while the plasmid system appears to target both plasmids and viral sequences, a distribution mirroring broader trends observed in other plasmid- and chromosome-encoded CRISPR systems. This observed targeting preference suggests a potential for complementarity that could support a model of cooperative immunity, where each system may protect its genetic \"owner\" from competition and, indirectly, the host.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf033"},"PeriodicalIF":0.0,"publicationDate":"2025-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12596717/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145490960","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-13eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf031
{"title":"Correction to: Avirulent Pseudomonas aeruginosa T3SS-negative strains belonging to Clade 5 produce variable quantities of secondary metabolites.","authors":"","doi":"10.1093/femsml/uqaf031","DOIUrl":"https://doi.org/10.1093/femsml/uqaf031","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1093/femsml/uqaf019.].</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf031"},"PeriodicalIF":0.0,"publicationDate":"2025-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12516122/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145294665","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-11eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf029
Víctor de Lorenzo, Paul B Rainey, Paul Williams, Zeynep Ceren Karahan, Puri López-García, Stipan Jonjić, Kenneth N Timmis
{"title":"Storm over science: predatory practices and the fight for research reliability.","authors":"Víctor de Lorenzo, Paul B Rainey, Paul Williams, Zeynep Ceren Karahan, Puri López-García, Stipan Jonjić, Kenneth N Timmis","doi":"10.1093/femsml/uqaf029","DOIUrl":"10.1093/femsml/uqaf029","url":null,"abstract":"<p><p>Scientific publishing faces a credibility crisis driven to a very large extent by predatory journals, paper mills, and exploitative open-access (OA) practices. Structural pressures-publish-or-perish culture, mandatory OA policies, and author publication charges-driven business models-fuel the proliferation of low-quality or fraudulent research, now exacerbated by artificial intelligence-generated content. This opinion, which aligns with a growing clamour from the research community-calls for an international journal accreditation system, guided by a transparent code of conduct and enforced by funding agencies, to restore integrity, prioritize quality over quantity for professional progression, and safeguard trust in scientific communication.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf029"},"PeriodicalIF":0.0,"publicationDate":"2025-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12539563/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145350321","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-08eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf030
Ana Natriashvili, Nahid Mohammadsadeghi, Eva Smudde, Bork Berghoff, Maximilian H Ulbrich, Hans-Georg Koch
{"title":"The small bacterial membrane protein YohP induces nucleoid condensation in <i>E. coli</i> and inhibits oligomerization of antimicrobial peptides.","authors":"Ana Natriashvili, Nahid Mohammadsadeghi, Eva Smudde, Bork Berghoff, Maximilian H Ulbrich, Hans-Georg Koch","doi":"10.1093/femsml/uqaf030","DOIUrl":"10.1093/femsml/uqaf030","url":null,"abstract":"<p><p>Prokaryotic organisms execute multiple stress response mechanisms in order to cope with rapidly changing environments. Some mechanisms respond to specific cues, such as the OxyR-dependent response to hydrogen peroxide or the SOS-response that is induced upon DNA-damage. These specific responses complement general mechanisms that respond to multiple and diverse stressors. One example is nucleoid condensation, which is a rapid and effective mechanism for genome protection and observed in response to various stresses, including entry into stationary phase. Recently, the upregulation of small membrane proteins (SMPs) in response to stress was observed, but details on how this emerging class of proteins modulate the stress response is largely unknown. Here, we demonstrate that the production of two SMPs, YohP and YncL, cause nucleoid condensation in <i>Escherichia coli</i>. Nucleoid condensation is the result of YohP-/YncL-induced sublethal membrane depolarization, which induces the phage-shock response and leads to a reduction of global protein synthesis. YohP production also prevents the oligomerization of the antimicrobial peptide magainin-2 in the <i>E. coli</i> membrane and reduces the metabolic activity of <i>E. coli</i> cells. Thus, the synthesis of YohP and likely of other SMPs potentially protects bacterial cells against some unfavorable conditions by shifting them into a metabolically silent state.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf030"},"PeriodicalIF":0.0,"publicationDate":"2025-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12542507/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145357085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-06eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf028
Jordan Vacheron, Clara M Heiman, Daniel Garrido-Sanz, Martine Caroff, Maryam Darabi, Christoph Keel
{"title":"Single nucleotide switches confer bacteriophage resistance to <i>Pseudomonas protegens</i>.","authors":"Jordan Vacheron, Clara M Heiman, Daniel Garrido-Sanz, Martine Caroff, Maryam Darabi, Christoph Keel","doi":"10.1093/femsml/uqaf028","DOIUrl":"10.1093/femsml/uqaf028","url":null,"abstract":"<p><p>Phage therapy offers a promising strategy against bacterial pathogens in medicine and agriculture, but the rise of phage-resistant bacteria presents a significant challenge to its sustainability. Here, we used an environmental model bacterium, <i>Pseudomonas protegens</i> CHA0, to investigate phage resistance mechanisms in laboratory conditions through genomic analysis of four phage-resistant variants (C2, C4, C17, C18). Whole-genome sequencing revealed frequent deletions, insertions, and single nucleotide substitutions, particularly in genes encoding enzymes involved in cell surface modifications. The T428P mutation in AlgC, a phosphoglucomutase, and the P229T substitution in YkcC, a glycosyltransferase, each conferred resistance by altering phage receptor accessibility while preserving bacterial fitness. These findings emphasize that subtle mutations in surface-modifying enzymes enable <i>P. protegens</i> to evolve resistance to bacteriophages without compromising their ecological performance.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf028"},"PeriodicalIF":0.0,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12532310/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145331065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-06eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf027
Felix Metz, Johanna Beilmann, Simon H Bats, Andreas Latoscha, Gregor Witte, Remco T A Megens, Karl-Peter Hopfner, Kaisa Thorell, Wolfgang Fischer, Laurent Terradot, Sebastian Suerbaum, Christine Josenhans
{"title":"Functional and intricate interaction network connecting <i>Helicobacter pylori</i> Cag type 4 secretion system surface proteins with outer membrane proteins HopQ and HopZ.","authors":"Felix Metz, Johanna Beilmann, Simon H Bats, Andreas Latoscha, Gregor Witte, Remco T A Megens, Karl-Peter Hopfner, Kaisa Thorell, Wolfgang Fischer, Laurent Terradot, Sebastian Suerbaum, Christine Josenhans","doi":"10.1093/femsml/uqaf027","DOIUrl":"10.1093/femsml/uqaf027","url":null,"abstract":"<p><p>The <i>Helicobacter pylori cag</i> pathogenicity island (<i>cag</i>PAI) encodes a complex virulence-associated type IV secretion system (CagT4SS). Recently, structural detail on the CagT4SS has been substantially improved by Cryo-EM. However, important structural and functional information is still missing. In the present study, we followed the hypothesis that <i>H. pylori</i> T4SS external proteins may form a surface-exposed assembly, together with non-CagT4SS proteins, which may be essential for T4SS function. Using interaction screens followed by biochemical and functional characterization, we have enhanced the knowledge about functional protein-protein interactions of the CagT4SS extracellular proteins. This comprises newly identified interactions of CagT4SS surface proteins, including the VirB2 homolog CagC, the VirB5 homolog CagL and CagN, with outer membrane proteins HopQ and HopZ. We have further quantitated direct, pH dependent, interactions of T4SS surface proteins with HopZ and HopQ, with host cell factors CEACAM and integrin, and self-interactions of both HopZ and HopQ. Utilizing chromosomal tag insertions in <i>H. pylori</i>, we detected surface-exposed colocalization of HopQ with T4SS components in the absence or, for HopQ, also in the presence of human gastric epithelial cells. Functionally antagonistic roles of HopQ and HopZ were uncovered in early proinflammatory human epithelial cell activation by the T4SS. In summary, we identified a network of interactions between <i>H. pylori</i> outer membrane proteins and CagT4SS surface proteins that are functionally relevant for T4SS-dependent transport processes. This study provides a valuable resource guiding future studies to refine structure and mechanistic roles of the surface-exposed portions of the CagT4SS.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf027"},"PeriodicalIF":0.0,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12542503/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145357051","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
microLifePub Date : 2025-10-03eCollection Date: 2025-01-01DOI: 10.1093/femsml/uqaf024
Luise Rentz, Lisa Hellwig, Sabine Schneider, Ruth A Schmitz
{"title":"Functional insights into Solo-Cas4 in <i>Methanosarcina mazei</i> Gö1.","authors":"Luise Rentz, Lisa Hellwig, Sabine Schneider, Ruth A Schmitz","doi":"10.1093/femsml/uqaf024","DOIUrl":"10.1093/femsml/uqaf024","url":null,"abstract":"<p><p>Solo-Cas4 homologs are Cas4-family proteins found outside of canonical CRISPR-Cas operons. Here, we present the biochemical characterization of Solo-Cas4 from <i>Methanosarcina mazei</i> Gö1. We found significantly upregulated <i>solo-cas4</i> transcript levels during stationary phase, while remaining constant under oxygen exposure, temperature shifts, high salt conditions or virus challenge. Heterologously expressed as a SUMO-fusion, the purified tag-free protein displays an absorption peak at 420 nm, indicative of a [4Fe-4S]-cluster. Size-exclusion-chromatography revealed that Solo-Cas4 forms a higher oligomeric complex, with an apparent molecular mass of 318 kDa. <i>In vitro</i> nuclease activity assays demonstrated that Solo-Cas4 cleaves metal-dependent linear dsDNA, with highest cleavage activity in the presence of Mn<sup>2+</sup>, followed by Mg<sup>2+</sup>, while Ca²⁺ and Cu²⁺ result in negligible cleavage. Isoleucine169 was identified to be crucial for catalysis, mutating it to alanine completely abolished nuclease activity. Mutating any of the four conserved cysteines-proposed to coordinate the [4Fe-4S]-cluster did not affect nuclease activity; however, it abolishes metal cluster binding. Supercoiled circular dsDNA was preferentially nicked by Solo-Cas4 in the presence of Mg<sup>2+</sup>, whereas Mn<sup>2+</sup> also led to linearization followed by complete degradation. Besides, ssDNA was cleaved by Solo-Cas4 but with lower activity. In agreement, Microscale thermophoresis analysis revealed strong dsDNA binding with highest affinity to supercoiled circular DNA, and weak ssDNA binding. Overall, these findings indicate that <i>M. mazei</i> Solo-Cas4 is a high oligomeric Cas4-family nuclease that preferentially targets supercoiled dsDNA and is upregulated during stationary growth.</p>","PeriodicalId":74189,"journal":{"name":"microLife","volume":"6 ","pages":"uqaf024"},"PeriodicalIF":0.0,"publicationDate":"2025-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12501428/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145253816","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}