Molecular Microbiology最新文献

筛选
英文 中文
ClpS Directs Degradation of N-Degron Substrates With Primary Destabilizing Residues in Mycolicibacterium smegmatis 在耻垢分枝杆菌中,ClpS用初级不稳定残基指导n -降解底物
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-12-03 DOI: 10.1111/mmi.15334
Christopher J. Presloid, Jialiu Jiang, Pratistha Kandel, Henry R. Anderson, Patrick C. Beardslee, Thomas M. Swayne, Karl R. Schmitz
{"title":"ClpS Directs Degradation of N-Degron Substrates With Primary Destabilizing Residues in Mycolicibacterium smegmatis","authors":"Christopher J. Presloid, Jialiu Jiang, Pratistha Kandel, Henry R. Anderson, Patrick C. Beardslee, Thomas M. Swayne, Karl R. Schmitz","doi":"10.1111/mmi.15334","DOIUrl":"https://doi.org/10.1111/mmi.15334","url":null,"abstract":"Drug-resistant tuberculosis infections are a major threat to global public health. The essential mycobacterial ClpC1P1P2 protease has received attention as a prospective target for novel antibacterial therapeutics. However, efforts to probe its function in cells are constrained by our limited knowledge of its physiological proteolytic repertoire. Here, we interrogate the role of mycobacterial ClpS in directing N-degron pathway proteolysis by ClpC1P1P2 in <i>Mycolicibacterium smegmatis</i>. Binding assays demonstrate that mycobacterial ClpS binds canonical primary destabilizing residues (Leu, Phe, Tyr, Trp) with moderate affinity. N-degron binding restricts the conformational flexibility of a loop adjacent to the ClpS N-degron binding pocket and strengthens ClpS•ClpC1 binding affinity ~30-fold, providing a mechanism for cells to prioritize N-degron proteolysis when substrates are abundant. Proteolytic reporter assays in <i>M. smegmatis</i> confirm degradation of substrates bearing primary N-degrons, but suggest that secondary N-degrons are absent in mycobacteria. This work expands our understanding of the mycobacterial N-degron pathway and identifies ClpS as a critical component for substrate specificity, providing insights that may support the development of improved Clp protease inhibitors.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"116 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142763487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Substrate Uptake by TonB-Dependent Outer Membrane Transporters tonb依赖性外膜转运体对底物的摄取
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-12-03 DOI: 10.1111/mmi.15332
Volkmar Braun
{"title":"Substrate Uptake by TonB-Dependent Outer Membrane Transporters","authors":"Volkmar Braun","doi":"10.1111/mmi.15332","DOIUrl":"https://doi.org/10.1111/mmi.15332","url":null,"abstract":"TonB is an essential component of an energy-generating system that powers active transport across the outer membrane (OM) of compounds that are too large or too scarce to diffuse through porins. The TonB-dependent OM transport proteins (TBDTs) consist of β barrels forming pores that are closed by plugs. The binding of TonB to TBDTs elicits plug movement, which opens the pores and enables nutrient translocation from the cell surface into the periplasm. TonB is also involved in the uptake of certain proteins, particularly toxins, through OM proteins that differ structurally from TBDTs. TonB binds to a sequence of five residues, designated as the TonB box, which is conserved in all TBDTs. Energy from the proton motive force (pmf) of the cytoplasmic membrane is transmitted to TonB by two proteins, ExbB and ExbD. These proteins form an energy-transmitting protein complex consisting of five ExbB proteins, forming a pore that encloses the ExbD dimer. This review discusses the structural changes that occur in TBDTs upon interaction with TonB, as well as the interaction of ExbB-ExbD with TonB, which is required to transmit the energy of the pmf and thereby open TBDT pores. TonB facilitates import of a wide range of substrates.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"13 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142763486","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Uncovering the Significance of JNK/AKT Axis in the Autophagic Regulation of Leishmania major Infection 揭示JNK/AKT轴在利什曼原虫感染自噬调控中的意义
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-12-03 DOI: 10.1111/mmi.15333
Vrushali Guhe, Shailza Singh
{"title":"Uncovering the Significance of JNK/AKT Axis in the Autophagic Regulation of Leishmania major Infection","authors":"Vrushali Guhe, Shailza Singh","doi":"10.1111/mmi.15333","DOIUrl":"https://doi.org/10.1111/mmi.15333","url":null,"abstract":"The role of autophagy in host induced by infection of parasites of the <i>Leishmania</i> genus remains inadequately understood. <i>Leishmania</i> parasites modulate host macrophages to promote its survival by inducing autophagy response in the host cell. In this study, we conducted an investigation of <i>L. major</i> infection, focusing on host autophagy processes where we reconstructed two mathematical models elucidating autophagy induction and inhibition processes and its impact on parasite survival. Our models presented systems modulatory dynamics of the parasite-mediated host autophagy. Our work highlighted the pivotal role of signaling molecules associated with the immune response which included signaling induced by Toll-like receptor (TLR), specifically through regulation of JNK and AKT. Both molecules emerged as key regulators of host autophagy process, highlighting that JNK/AKT signaling axis may be a potential avenue for innovative therapeutic approaches in targeting leishmaniasis. Also, ATG16L complex was identified as a critical determinant in shaping the course of leishmanial infection through formation of autophagosomes. Through in vitro analyses in differentiated human monocyte cell line, we observed an increase in nitric oxide synthase (iNOS) concentration upon autophagy inhibition, while autophagy induction resulted in decreased iNOS concentration. This suggested that autophagy induction favors parasite survival in the host, potentially by providing a nutrient source that may be advantageous for the parasite. Inhibition of host autophagy promoted parasite elimination. Hence, our work proposed an avenue for strategically blocking host autophagy which enumerates a targeted approach for combating leishmaniasis.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"14 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142763144","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Capsular Polysaccharide Production in Bacteria of the Mycoplasma Genus: A Huge Diversity of Pathways and Synthases for So-Called Minimal Bacteria. 支原体属细菌的囊状多糖生产:所谓最小细菌的途径和合成酶的巨大多样性。
IF 2.6 2区 生物学
Molecular Microbiology Pub Date : 2024-12-01 Epub Date: 2024-10-30 DOI: 10.1111/mmi.15325
Manon Vastel, Corinne Pau-Roblot, Séverine Ferré, Véronique Tocqueville, Chloé Ambroset, Corinne Marois-Créhan, Anne V Gautier-Bouchardon, Florence Tardy, Patrice Gaurivaud
{"title":"Capsular Polysaccharide Production in Bacteria of the Mycoplasma Genus: A Huge Diversity of Pathways and Synthases for So-Called Minimal Bacteria.","authors":"Manon Vastel, Corinne Pau-Roblot, Séverine Ferré, Véronique Tocqueville, Chloé Ambroset, Corinne Marois-Créhan, Anne V Gautier-Bouchardon, Florence Tardy, Patrice Gaurivaud","doi":"10.1111/mmi.15325","DOIUrl":"10.1111/mmi.15325","url":null,"abstract":"<p><p>Mycoplasmas are wall-less bacteria with many species spread across various animal hosts in which they can be pathogenic. Despite their reduced anabolic capacity, some mycoplasmas are known to secrete hetero- and homopolysaccharides, which play a role in host colonization through biofilm formation or immune evasion, for instance. This study explores how widespread the phenomenon of capsular homopolysaccharide secretion is within mycoplasmas, and investigates the diversity of both the molecules produced and the synthase-type glycosyltransferases responsible for their production. Fourteen strains representing 14 (sub)species from four types of hosts were tested in vitro for their polysaccharide secretion using both specific (immunodetection) and nonspecific (sugar dosage) assays. We evidenced a new, atypical homopolymer of β-(1 → 6)-glucofuranose (named glucofuranan) in the human pathogen Mycoplasma (M.) fermentans, as well as a β-(1 → 6)-glucopyranose polymer for the turkey pathogen M. iowae and galactan (β-(1 → 6)-galactofuranose) and β-(1 → 2)-glucopyranose for M. bovigenitalium infecting ruminants. Sequence and phylogenetic analyses revealed a huge diversity of synthases from varied Mycoplasma species. The clustering of these membrane-embedded glycosyltransferases into three main groups was only partially correlated to the structure of the produced homopolysaccharides.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"866-878"},"PeriodicalIF":2.6,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11658790/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142546490","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The Complex and Challenging World of the Host–Pathogen Interaction 宿主与病原体相互作用的复杂而充满挑战的世界
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-25 DOI: 10.1111/mmi.15310
Marcel I. Ramirez
{"title":"The Complex and Challenging World of the Host–Pathogen Interaction","authors":"Marcel I. Ramirez","doi":"10.1111/mmi.15310","DOIUrl":"https://doi.org/10.1111/mmi.15310","url":null,"abstract":"","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"6 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697063","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Comparative Multi-Omics Survey Reveals Novel Specialized Metabolites and Biosynthetic Gene Clusters Under GacS Control in Pseudomonas donghuensis Strain SVBP6 多重组学比较调查揭示了东湖假单胞菌 SVBP6 菌株中受 GacS 控制的新型特化代谢物和生物合成基因簇
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-15 DOI: 10.1111/mmi.15329
Federico Matías Muzio, Corri D. Hamilton, Paolo Stincone, Betina Agaras, Cara H. Haney, Daniel Petras, Claudio Valverde
{"title":"Comparative Multi-Omics Survey Reveals Novel Specialized Metabolites and Biosynthetic Gene Clusters Under GacS Control in Pseudomonas donghuensis Strain SVBP6","authors":"Federico Matías Muzio, Corri D. Hamilton, Paolo Stincone, Betina Agaras, Cara H. Haney, Daniel Petras, Claudio Valverde","doi":"10.1111/mmi.15329","DOIUrl":"https://doi.org/10.1111/mmi.15329","url":null,"abstract":"In <i>Pseudomonas donghuensis</i> SVBP6, isolated from an agricultural field, the well-conserved Gac-Rsm pathway upregulates biosynthesis of the antifungal compound 7-hydroxytropolone (7-HT). However, 7-HT does not fully explain the strain's Gac-Rsm-dependent antimicrobial activity. Here, we combined comparative transcriptomic, proteomic, and metabolomic approaches to identify novel GacS-dependent biosynthetic gene clusters (BGC) and/or extracellular specialized metabolites. Our data revealed a broad impact of GacS on gene expression and extracellular metabolite profile of SVBP6. At both the mRNA and polypeptide levels, specialized metabolism was the main affected functional category in the <i>gacS</i> mutant. The major extracellular MS/MS spectral families promoted by GacS were fatty acid amides, fatty acids, and alkaloids. GacS was required for the production of the antimicrobial compound pseudoiodinine and to activate expression of the corresponding BGC. We also detected GacS-dependent production of 2,3,4-trihydro-β-carboline-1-one, which may add to the antimicrobial arsenal of SVBP6. Furthermore, transcriptomics and proteomics pinpointed several GacS-activated BGCs that had escaped <i>in silico</i> genome mining tools. Altogether, comparative multi-omics analyses of <i>gacS</i> loss-of-function mutants in <i>Pseudomonas</i> isolates are a promising strategy to uncover bioactive metabolites and/or their BGCs. Discovery of novel natural products is important for harnessing the potential of microbiota to improve crop plant growth and health.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"16 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142637584","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Bacterial Organelles in Iron Physiology 铁生理学中的细菌细胞器
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-15 DOI: 10.1111/mmi.15330
Kristina M. Ferrara, Kuldeepkumar R. Gupta, Hualiang Pi
{"title":"Bacterial Organelles in Iron Physiology","authors":"Kristina M. Ferrara, Kuldeepkumar R. Gupta, Hualiang Pi","doi":"10.1111/mmi.15330","DOIUrl":"https://doi.org/10.1111/mmi.15330","url":null,"abstract":"Bacteria were once thought to be simple organisms, lacking the membrane-bound organelles found in eukaryotic cells. However, recent advancements in microscopy have changed this view, revealing a diverse array of organelles within bacterial cells. These organelles, surrounded by lipid bilayers, protein-lipid monolayers, or proteinaceous shells, play crucial roles in facilitating biochemical reactions and protecting cells from harmful byproducts. Unlike eukaryotic organelles, which are universally present, bacterial organelles are species-specific and induced only under certain conditions. This review focuses on the bacterial organelles that contain iron, an essential micronutrient for all life forms but potentially toxic when present in excess. To date, three types of iron-related bacterial organelles have been identified: two membrane-bound organelles, magnetosomes and ferrosomes, and one protein-enclosed organelle, the encapsulated ferritin-like proteins. This article provides an updated overview of the genetics, biogenesis, and physiological functions of these organelles. Furthermore, we discuss how bacteria utilize these specialized structures to adapt, grow, and survive under various environmental conditions.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"9 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142637585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Converging Roles of the Metal Transporter SMF11 and the Ferric Reductase FRE1 in Iron Homeostasis of Candida albicans 金属转运体 SMF11 和铁还原酶 FRE1 在白色念珠菌铁平衡中的共同作用
IF 3.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-11 DOI: 10.1111/mmi.15326
Naisargi K. Patel, Marika S. David, Shuyi Yang, Ritu Garg, Hongyu Zhao, Brendan P. Cormack, Valeria C. Culotta
{"title":"Converging Roles of the Metal Transporter SMF11 and the Ferric Reductase FRE1 in Iron Homeostasis of Candida albicans","authors":"Naisargi K. Patel, Marika S. David, Shuyi Yang, Ritu Garg, Hongyu Zhao, Brendan P. Cormack, Valeria C. Culotta","doi":"10.1111/mmi.15326","DOIUrl":"https://doi.org/10.1111/mmi.15326","url":null,"abstract":"Pathogenic fungi must appropriately sense the host availability of essential metals such as Fe. In <i>Candida albicans</i> and other yeasts, sensing of Fe involves mitochondrial Fe-S clusters. Yeast mutants for Fe-S cluster assembly sense Fe limitation even when Fe is abundant and hyperaccumulate Fe. We observe this same disrupted Fe sensing with <i>C. albicans</i> mutants of SMF11, a NRAMP transporter of divalent metals. Mutants of <i>smf11</i> hyperaccumulate both Mn and Fe and the elevated Mn is secondary to Fe overload. As with Fe-S biogenesis mutants, <i>smf11∆/∆</i> mutants show upregulation of ferric reductases that are normally repressed under high Fe, and Fe import is activated. However, unlike Fe-S biogenesis mutants, <i>smf11∆/∆</i> mutants show no defects in mitochondrial Fe-S enzymes. Intriguingly, this exact condition of disrupted Fe sensing without inhibiting Fe-S clusters occurs with <i>C. albicans fre1∆/∆</i> mutants encoding a ferric reductase. Mutants of <i>fre1</i> and <i>smf11</i> display similar perturbations in the cell wall, in filamentation and in the ROS burst of morphogenesis, a Fe-dependent process. As with FRE1, SMF11 is important for virulence in a mouse model for disseminated candidiasis. We propose a model in which FRE1 and SMF11 operate outside the mitochondrial Fe-S pathway to donate ferrous Fe for Fe sensing.","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":"2 1","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142599927","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Genetic analysis of translation initiation in bacteria: An initiator tRNA-centric view. 细菌翻译启动的遗传分析:以启动子 tRNA 为中心的观点。
IF 2.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-01 Epub Date: 2024-02-27 DOI: 10.1111/mmi.15243
Kuldeep Lahry, Madhurima Datta, Umesh Varshney
{"title":"Genetic analysis of translation initiation in bacteria: An initiator tRNA-centric view.","authors":"Kuldeep Lahry, Madhurima Datta, Umesh Varshney","doi":"10.1111/mmi.15243","DOIUrl":"10.1111/mmi.15243","url":null,"abstract":"<p><p>Translation of messenger RNA (mRNA) in bacteria occurs in the steps of initiation, elongation, termination, and ribosome recycling. The initiation step comprises multiple stages and uses a special transfer RNA (tRNA) called initiator tRNA (i-tRNA), which is first aminoacylated and then formylated using methionine and N<sup>10</sup>-formyl-tetrahydrofolate (N<sup>10</sup>-fTHF), respectively. Both methionine and N<sup>10</sup>-fTHF are produced via one-carbon metabolism, linking translation initiation with active cellular metabolism. The fidelity of i-tRNA binding to the ribosomal peptidyl-site (P-site) is attributed to the structural features in its acceptor stem, and the highly conserved three consecutive G-C base pairs (3GC pairs) in the anticodon stem. The acceptor stem region is important in formylation of the amino acid attached to i-tRNA and in its initial binding to the P-site. And, the 3GC pairs are crucial in transiting the i-tRNA through various stages of initiation. We utilized the feature of 3GC pairs to investigate the nuanced layers of scrutiny that ensure fidelity of translation initiation through i-tRNA abundance and its interactions with the components of the translation apparatus. We discuss the importance of i-tRNA in the final stages of ribosome maturation, as also the roles of the Shine-Dalgarno sequence, ribosome heterogeneity, initiation factors, ribosome recycling factor, and coevolution of the translation apparatus in orchestrating a delicate balance between the fidelity of initiation and/or its leakiness to generate proteome plasticity in cells to confer growth fitness advantages in response to the dynamic nutritional states.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"772-788"},"PeriodicalIF":2.6,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139972680","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3SAL Compete for Occupancy. 体内交联揭示了沙门氏菌分裂体中 PBP3 和 PBP3SAL 竞相占据的情况。
IF 2.6 2区 生物学
Molecular Microbiology Pub Date : 2024-11-01 Epub Date: 2024-09-04 DOI: 10.1111/mmi.15309
Sónia Castanheira, David López-Escarpa, Alberto Paradela, Francisco García-Del Portillo
{"title":"In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3<sub>SAL</sub> Compete for Occupancy.","authors":"Sónia Castanheira, David López-Escarpa, Alberto Paradela, Francisco García-Del Portillo","doi":"10.1111/mmi.15309","DOIUrl":"10.1111/mmi.15309","url":null,"abstract":"<p><p>Bacterial cell division is orchestrated by proteins that assemble in dynamic complexes collectively known as the divisome. Essential monofunctional enzymes with glycosyltransferase or transpeptidase (TPase) activities, FtsW and FtsI respectively, engage in the synthesis of septal peptidoglycan (sPG). Enigmatically, Salmonella has two TPases that can promote cell division independently: FtsI (PBP3) and the pathogen-specific paralogue PBP3<sub>SAL</sub>. How Salmonella regulates the assembly of the sPG synthase complex with these two TPases, is unknown. Here, we characterized Salmonella division complexes in wild-type cells and isogenic mutants lacking PBP3 or PBP3<sub>SAL</sub>. The complexes were cross-linked in vivo and pulled down with antibodies recognizing each enzyme. Proteomics of the immunoprecipitates showed that PBP3 and PBP3<sub>SAL</sub> do not extensively cross-link in wild type cells, supporting the presence of independent complexes. More than 40 proteins cross-link in complexes in which these two TPases are present. Those identified with high scores include FtsA, FtsK, FtsQLB, FtsW, PBP1B, SPOR domain-containing proteins (FtsN, DedD, RlpA, DamX), amidase activators (FtsX, EnvC, NlpD) and Tol-Pal proteins. Other cross-linked proteins are the protease Prc, the elongasome TPase PBP2 and, D,D-endo- and D,D-carboxypeptidases. PBP3 and PBP3<sub>SAL</sub> localize at midcell and compete for occupying the division complex in response to environmental cues. Thus, a catalytic-dead PBP3<sub>SAL</sub>-S300A variant impairs cell division in a high osmolarity and acidic condition in which it is produced at levels exceeding those of PBP3. Salmonella may therefore exploit an 'adjustable' divisome to exchange TPases for ensuring cell division in distinct environments and, in this manner, expand its colonization capacities.</p>","PeriodicalId":19006,"journal":{"name":"Molecular Microbiology","volume":" ","pages":"797-818"},"PeriodicalIF":2.6,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11586514/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142133258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信