{"title":"TrbA binds and locks a sliding clamp KorB to repress transcription on multi-drug resistance plasmids.","authors":"Thomas C McLean, Govind Chandra, Tung B K Le","doi":"10.1128/jb.00286-26","DOIUrl":"10.1128/jb.00286-26","url":null,"abstract":"<p><p>Precise regulation of gene expression is essential for all living systems. Genes encoded on mobile genetic elements such as conjugative plasmids are also highly regulated to ensure stable inheritance, successful horizontal transfer, and adaptation to diverse bacterial hosts. The multi-drug resistance plasmid RK2 encodes an intricate regulatory network centered on the ParB-CTPase family protein KorB, which functions in both plasmid segregation and global gene regulation. We recently showed that KorB acts as a CTP-dependent DNA-sliding clamp that can be converted into a transcriptional repressor through direct interaction with the DNA-binding protein KorA. This clamp sliding-and-locking mechanism by KorAB enables highly effective transcriptional repression. Here, we investigate whether a third transcriptional regulator on the RK2 plasmid, TrbA, operates through a similar mechanism. Using a combination of structural prediction, biochemistry, and <i>in vivo</i> transcriptional assays, we provide evidence that TrbA also directly interacts with KorB and functions as a clamp-locking factor. This KorB-TrbA interaction is mediated by a conserved aromatic interface that enables strong cooperative transcriptional repression. Disruption of this interface abolishes synergy, indicating that direct protein-protein interaction underpins KorB-TrbA cooperativity. Finally, bioinformatic analysis of a large plasmid database reveals that the tripartite KorB-KorA-TrbA system is present on numerous plasmids. Together, our findings establish TrbA as a <i>bona fid</i>e KorB co-repressor and demonstrate how a single sliding clamp protein can integrate multiple partners to evolve a complex transcriptional regulatory network.IMPORTANCEPrecise regulation of gene expression ensures gene products are produced at the right time and in the right amounts. Recent works uncovered a new mechanism of bacterial gene regulation based on a clamp sliding and locking in a multi-drug resistance plasmid, RK2. KorB functions as a CTP-dependent DNA-sliding clamp capable of traveling over a long genomic distance. Sliding KorB is captured and locked in place by a partner protein, KorA, forming a stable complex at target promoters to repress transcription. Here, we show that another RK2 regulator, TrbA, also uses this clamp sliding-locking mechanism, and identify an aromatic interface enabling TrbA-KorB-mediated transcriptional repression. Our findings show how a single sliding clamp integrates multiple partners to build a complex transcriptional regulatory network.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0028626"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584720/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148706662","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}
Samyabrata Sen, E C Henderson, Ferran Garcia-Pichel, Mohammed Kaplan, Abhishek Shrivastava
{"title":"Correction for Sen et al., \"Distinct motors, shared mechanics: unifying principles of microbial gliding\".","authors":"Samyabrata Sen, E C Henderson, Ferran Garcia-Pichel, Mohammed Kaplan, Abhishek Shrivastava","doi":"10.1128/jb.00215-26","DOIUrl":"10.1128/jb.00215-26","url":null,"abstract":"","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0021526"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584735/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148818509","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}
Jinger Lei, Misaki Foster, Emery Ng, Erin S Gloag, Xiaogang Wang
{"title":"Extracellular membrane vesicles-previously unrecognized components of <i>Staphylococcus aureus</i> biofilms.","authors":"Jinger Lei, Misaki Foster, Emery Ng, Erin S Gloag, Xiaogang Wang","doi":"10.1128/jb.00210-26","DOIUrl":"10.1128/jb.00210-26","url":null,"abstract":"<p><p><i>Staphylococcus aureus</i> is a leading cause of biofilm-associated infections, in which communities of bacterial cells are encased in an extracellular matrix composed of polysaccharides, proteins, and extracellular DNA (eDNA) that protect bacteria from host immune defense and antibiotics. Despite their importance, the mechanisms by which matrix components are released from bacterial cells and incorporated into the biofilm matrix remain poorly understood. Using a drip-flow biofilm system, we showed that membrane vesicles (MVs) were associated with the biofilm matrix formed by <i>S. aureus</i> clinical isolate MN8. Proteomic analysis of biofilm matrix proteins and purified MVs showed that biofilm-derived MVs carried cytoplasmic, membrane, and extracellular proteins that closely resembled the protein composition of the biofilm matrix, but differed significantly from MVs produced by planktonic cultures. Biofilm-derived MVs carried significantly higher levels of DNA than MVs from planktonic cultures, and MV-associated DNA was sensitive to DNase treatment, suggesting that eDNA is primarily associated with the MV surface. Although strain MN8 is known to form polysaccharide-dependent biofilms, exogenously added DNase or proteinase K significantly impaired biofilm formation and integrity. Importantly, supplementation with biofilm-derived MVs, but not MVs from planktonic cultures, significantly restored biofilm formation in enzyme-treated static cultures. Together, these findings provide evidence that <i>S. aureus</i> MVs are generated within biofilms, and that these MVs serve as an important resource of matrix components and contribute to biofilm formation.</p><p><strong>Importance: </strong>Extracellular membrane vesicles (MVs) are important mediators of intercellular communication and have been implicated in the bacterial physiology and pathogenesis. MVs in fungi and gram-negative bacteria mediate key biofilm processes, such as formation and structural maintenance. However, MV production and function in biofilm formation in gram-positive bacteria have remained largely unexplored. Here, we report for the first time the purification and characterization of MVs derived from <i>Staphylococcus aureus</i> biofilms. Our studies demonstrate that <i>S. aureus</i> MVs are important components of the biofilm matrix that contribute to biofilm formation by serving as carriers of key matrix components. This work advances our limited understanding of MVs in gram-positive bacteria and reveals a previously unrecognized mechanism contributing to <i>S. aureus</i> biofilm formation.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0021026"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584710/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148684604","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}
Saher Shahid, Daniel Lundin, Inna Rozman Grinberg, Britt-Marie Sjöberg
{"title":"Ribonucleotide reductase repression: a mutational study of NrdR-binding motifs.","authors":"Saher Shahid, Daniel Lundin, Inna Rozman Grinberg, Britt-Marie Sjöberg","doi":"10.1128/jb.00274-26","DOIUrl":"10.1128/jb.00274-26","url":null,"abstract":"<p><p>The prevalent transcriptional repressor NrdR binds to highly conserved sequences in the promoter regions of prokaryotic operons encoding the essential enzyme ribonucleotide reductase. The NrdR-binding sites consist of two partially palindromic 16 bp sequences (NrdR boxes) separated by a 15-16 bp linker sequence. We have assessed the requirement of both boxes for binding, the propensity of different NrdRs to bind to heterologous binding sites, and that the linker sequence is only limited to length and not sequence conservation. As we have observed several deviations from the conserved sequences of the NrdR boxes, we have tested the conservation requirements of individual base pairs in the NrdR boxes using a synthetic DNA fragment (Synt DNA) to which the NrdR proteins from the actinomycete <i>Streptomyces coelicolor</i> and the gammaproteobacterium <i>Escherichia coli</i> bind equally well as to their homologous binding sites. By introducing isolated mutations to Synt DNA and testing the binding capacity of NrdR from <i>S. coelicolor</i> and <i>E. coli</i>, we expand our understanding of what criteria are needed to build a functional binding site for the NrdR repressor. Our results enable more precise identification of NrdR-binding sites across bacterial genomes, which can be used to explore NrdR and its regulons as potential targets for the development of novel antimicrobials.IMPORTANCEThe transcriptional repressor NrdR is strictly prokaryotic, occurring in 77% of bacterial genomes, and 22% of archaeal genomes. It binds to highly conserved sequences in the promoter regions of the genes encoding the essential enzyme ribonucleotide reductase that provides cells with <i>de novo</i> building blocks for DNA synthesis. Repression of ribonucleotide reductase expression leads to a lack of replication and cell proliferation. In this report, we have characterized in detail the generality of the partially palindromic sequences constituting the NrdR-binding site. As NrdR controls the sole <i>de novo</i> pathways for production of DNA building blocks in bacteria and not in eukaryotes, our results will facilitate screens for novel antimicrobials utilizing the NrdR protein and its homologous regulons in pathogenic bacteria.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0027426"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584703/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148828650","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}
Rui Zhan, Han Gong, Ying Li, Yuanyuan Cui, Xiangdong Chen, Joe Lutkenhaus, Shishen Du
{"title":"RodZ acts through MreBCD to activate the elongasome in <i>Escherichia coli</i>.","authors":"Rui Zhan, Han Gong, Ying Li, Yuanyuan Cui, Xiangdong Chen, Joe Lutkenhaus, Shishen Du","doi":"10.1128/jb.00594-25","DOIUrl":"10.1128/jb.00594-25","url":null,"abstract":"<p><p>Most bacteria are surrounded by a peptidoglycan (PG) matrix that maintains cell shape and provides protection against turgor pressure. In many rod-shaped bacteria, synthesis of PG along the cell cylinder is organized by the elongasome, also called the rod complex, which consists of six highly conserved proteins, including the actin-like MreB, the PG synthase complex RodA-PBP2, and three regulatory membrane proteins, MreC, MreD, and RodZ. However, how these proteins interact with each other to form the elongasome and synthesize lateral PG remains elusive. In this study, by characterizing MreC mutations affecting elongasome activity in <i>Escherichia coli</i>, we provide evidence that MreC alternates between an active and an inactive state, and these mutations affect MreC interaction with PBP2. We also find that RodZ interacts with MreC via a periplasmic region, and disruption of this interaction compromises elongasome function. Additionally, we show that the cytoplasmic region of RodZ, which interacts with MreB, works synergistically with activating MreC mutations to promote rod-shaped formation. These results indicate that RodZ activates the elongasome by initiating two signaling cascades, one in the periplasm via MreCD, and another in the cytoplasm through MreB. This role of RodZ in regulating elongasome activity is analogous to that of FtsN in activating the divisome, suggesting that the mechanisms governing the activation of PG synthesis in cell elongation and division are similar in <i>E. coli</i>.</p><p><strong>Importance: </strong>The elongasome, or rod complex, mediates lateral peptidoglycan (PG) synthesis during cell elongation in many rod-shaped bacteria. It consists of the cytoskeletal protein MreB, the peptidoglycan synthase RodA-PBP2, and three regulatory proteins MreCD and RodZ. Although it has been extensively studied, how its activity is controlled remains incompletely understood. Here, we reveal the roles of MreCD and RodZ in regulating elongasome activity in <i>Escherichia coli</i>. Our results indicate that RodZ triggers lateral peptidoglycan synthesis by interacting with MreB in the cytoplasm and MreCD in the periplasm. These interactions likely switch MreBCD to the active state, such that they can stimulate the activity of the RodA-PBP2 complex. This regulatory mechanism resembles the activation mechanism of the divisome that mediates septal peptidoglycan synthesis.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0059425"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584716/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148706664","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":"Dimensional analysis as a tool for biofilm comparative analysis: bridging the interdisciplinary divides.","authors":"Chelsea M Middleton, A-Andrew D Jones","doi":"10.1128/jb.00188-26","DOIUrl":"10.1128/jb.00188-26","url":null,"abstract":"<p><p>Biofilms are the predominant lifestyle for bacteria. Biofilm abundance makes understanding their behavior important for different research domains. These domains can have different information and reporting standards. Information reporting standards have been proposed for some biofilm research methods. Standard methods and consensus standards have also been promulgated. We propose dimensional analysis to encourage abundant information reporting and facilitate comparative analysis. Dimensional analysis utilizes physical system parameters to generate generalizable model data. We review dimensionless quantities that can be applied to biofilm studies. We suggest dimensionless quantities for existing standards, with three examples using dimensional analysis to quantitatively compare literature data.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0018826"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584748/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148684572","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}
Marco N Allemann, Leah H Hochanadel, Delyana P Vasileva, Joshua K Michener
{"title":"Horizontal transfer of chromosomal DNA mediated by an integrative and conjugative element generates frequent localized recombination in <i>Novosphingobium aromaticivorans</i>.","authors":"Marco N Allemann, Leah H Hochanadel, Delyana P Vasileva, Joshua K Michener","doi":"10.1128/jb.00175-26","DOIUrl":"10.1128/jb.00175-26","url":null,"abstract":"<p><p>Horizontal gene transfer is an important evolutionary process by which DNA is exchanged between cells that are physically co-located but not direct evolutionary descendants. Horizontal transfer of highly divergent DNA is relatively easy to detect and can produce major phenotypic changes, exemplified by the acquisition of antibiotic resistance determinants. However, transfer of high-identity DNA, for example, between strains of the same species, is likely to be more frequent, harder to detect, and highly impactful in aggregate. In this work, we demonstrate that soil isolates of the alphaproteobacterium <i>Novosphingobium aromaticivorans</i> can exchange chromosomal DNA, leading to multiple unselected recombination events spanning approximately 10% of the chromosome. Chromosomal recombination was directional and more efficient near an integrative and conjugative element (ICE), and required a relaxase found in the ICE. Recombination could not be observed in strains from closely related <i>Novosphingobium</i> species. In combination, these results suggest that ICE-mediated recombination can efficiently recombine DNA within <i>N. aromaticivorans</i>, increasing the adaptive potential of the species while also enforcing species boundaries through preferential intraspecific recombination.</p><p><strong>Importance: </strong>Horizontal gene transfer is a key process in bacterial evolution. Mechanisms for transfer of mobile genetic elements are well-characterized, but less is known about how chromosomal DNA is recombined. In this work, we demonstrate that integrative and conjugative elements can efficiently recombine chromosomal DNA between strains of <i>Novosphingobium aromaticivorans</i> but not between different <i>Novosphingobium</i> species. We conclude that integrative and conjugative element-mediated chromosomal recombination can be an important adaptive mechanism within a species, due to its ability to recombine nearby chromosomal alleles, but also serves to delineate species-specific gene pools as a result of its limited phylogenetic range.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0017526"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584701/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148684560","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>Pseudomonas aeruginosa</i>: a model system for studying the behavior of unbiased flagellar motors.","authors":"Zhengyu Wu, Maojin Tian, Sanyuan Fu, Rongjing Zhang, Junhua Yuan","doi":"10.1128/jb.00254-26","DOIUrl":"10.1128/jb.00254-26","url":null,"abstract":"<p><p>The flagellar motor of <i>Pseudomonas aeruginosa</i> operates in a near-unbiased manner, extending the classical paradigm established by <i>Escherichia coli</i>. Rather than altering rotational bias, <i>P. aeruginosa</i> achieves chemotaxis by symmetrically modulating the dwell times of the two rotational states. This strategy is associated with a mechanically adaptive dual-stator architecture (MotAB and MotCD) and is further modulated by c-di-GMP signaling and auxiliary proteins such as FliL and MotY. At the molecular level, the distinctive reversal behavior is thought to arise from the unique response of the switch complex (located on the rotor) to phosphorylated CheY, which alters switching kinetics rather than rotational bias. These features collectively give rise to distinct swimming behaviors, including a \"wrap\" state that facilitates three-dimensional reorientation. This system reveals general principles of how molecular machines balance speed, torque, and switching in complex environments.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0025426"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584743/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148712640","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}
Marcelle C Dos Santos Ferreira, Timothy G Stephens, Shaun R Brinsmade
{"title":"In <i>Staphylococcus aureus</i>, MbcS is a refunctionalized acyl-CoA synthetase that confers a fitness advantage during intra-species competition.","authors":"Marcelle C Dos Santos Ferreira, Timothy G Stephens, Shaun R Brinsmade","doi":"10.1128/jb.00185-26","DOIUrl":"10.1128/jb.00185-26","url":null,"abstract":"<p><p><i>Staphylococcus aureus</i> is one of the most frequently co-isolated pathogens in polymicrobial infections, where interspecies interactions contribute to enhanced virulence, persistence, and antimicrobial tolerance. Nutrient availability plays a central role in these interactions as microorganisms compete for resources to sustain essential cellular processes. For instance, branched-chain amino acids (BCAAs) are critical for protein synthesis, and valine synthesis pathway precursors are essential for energy production. In <i>S. aureus</i>, BCAAs are also the precursors for branched-chain fatty acids (BCFAs), the dominant fatty acids in the <i>S. aureus</i> membrane. We previously identified a second pathway that uses branched-chain carboxylic acids (BCCAs) and the high-affinity acyl-CoA synthetase MbcS to catalyze the formation of primers for BCFA synthesis. However, the physiological role of this pathway and the conditions triggering its activation remain unclear. Here, we show that <i>mbcS</i> is restricted to <i>S. aureus</i> and closely related human-associated staphylococci. Phylogenetic analyses suggest that MbcS arose from a refunctionalization event and represents a non-orthologous replacement for the phosphotransbutyrylase (Ptb) and butyrate kinase (Buk) enzymes. Consistent with this model, Ptb and Buk from <i>Staphylococcus pseudintermedius</i> catalyze the formation of branched-chain acyl-CoAs from BCCAs, but only at high substrate concentrations. We further show that <i>mbcS</i> expression is upregulated in a CodY-deficient strain, implicating this pathway in BCAA-limited conditions. In support, we show that MbcS is required for optimal fitness during intra-species competition. Together, our findings support a model in which the MbcS-dependent pathway enables <i>S. aureus</i> to scavenge BCFA precursors under nutrient-limited conditions, providing a competitive advantage in polymicrobial environments.</p><p><strong>Importance: </strong><i>Staphylococcus aureus</i> is a major contributor to polymicrobial infections, where competition for nutrients can influence bacterial physiology and survival. A deeper understanding of how <i>S. aureus</i> adapts to nutrient limitation is therefore essential to explain its success as a human pathogen. In <i>S. aureus</i>, the acyl-CoA synthetase MbcS supports branched-chain fatty acid (BCFA) synthesis from branched-chain amino acid (BCAA)-derived carboxylic acids and aldehydes, which are released into the environment as by-products of bacterial metabolism. Herein, we provide evidence that <i>S. aureus</i> acquired the acyl-CoA synthetase MbcS as an adaptive trait. This metabolic innovation allows this bacterium to maintain membrane homeostasis under nutrient limitation and compete against neighboring bacteria. Our findings highlight an adaptive strategy that may contribute to the persistence of <i>S. aureus</i> in polymicrobial infections.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0018526"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584741/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148828745","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}