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Bacterial Cell Envelope Biosynthesis
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Bacterial Cell Envelope Biosynthesis

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (31 August 2022) | Viewed by 17355

Special Issue Editor

Prof. Dr. Tanneke Den Blaauwen

E-Mail Website
Guest Editor
Bacterial Cell Biology and Physiology, Swammerdam Institute for Life Sciences, Faculty of Science, University of Amsterdam, Amsterdam, The Netherlands
Interests: E. coli; bacterial morphogenesis; peptidoglycan synthesis/hydrolysis; fluorescence microscopy; image analysis; Forster Resonsance Energy Transfer (FRET); protein interactions; protein translocation; divsion proteins; elongation proteins; outer membrane proteins; fluorescence proteins; symbionts; antibiotic targets

Special Issue Information

Dear Colleagues,

As you might have noticed, the International Journal of Molecular Science is publishing more and more manuscripts on bacterial morphogenesis and bacteriology. The importance of bacterial species diversity for the wellbeing and health of the world ‘s ecosystems, including its human inhabitants, is by now clearly established. Consequently, the notion that the range of bacterial species whose morphogenesis is investigated at a molecular level needs to be expanded beyond the canonical Escherichia coli and Bacillus subtilis is gaining momentum in our community. In addition, it is becoming more and more clear that the regulation of envelope growth and division is very complex and that the involved protein complexes are not isolated entities, but part of communicating networks. The most successful antibiotics that apparently just inhibited the activity of a single protein type, appear to affect usually multiple process upon closer inspection. Limiting our knowledge to one aspect of morphogenesis (i.e., peptidoglycan syntheses) is no longer possible without knowledge on the other cross-talking processes. The development of successful antibiotics and antibiotic screening assays will benefit from molecular knowledge of this cross-talking. To illustrate these developments, I would like to collect manuscripts for a Special Issue on bacterial morphogenesis that encompasses multiple bacterial species and any process that is related to bacterial growth and division on a molecular level.

The publication procedure of IJMS is simpler than for most other journals. Simply paste your text into the journal's formatted file and the paper is ready for review and, if accepted, publication. As an editor of the journal, I make sure that each paper in my care is thoroughly reviewed by two reviewers and, in case of doubt, a third reviewer is invited. The journal has the DOAJ Seal (The DOAJ Seal is awarded to journals that demonstrate best practice in open access publishing. Around 10% of journals indexed in DOAJ have been awarded the Seal.)

The impact factor of IJMS is 5.9 at present.

I hope that you will be inspired to submit a manuscript to this Special Issue.

Prof. Dr. Tanneke Den Blaauwen
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

 

Keywords

  • outer membrane synthesis regulation
  • Gram negative bacteria including Actinobacteria
  • Gram positive bacteria
  • Archaea
  • envelop biosynthesis
  • peptidoglycan biosynthesis
  • transenvelop protein complexes
  • cell division
  • protein transport
  • microscopy
  • assays
  • in vitro and in vivo

Published Papers (6 papers)

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Research

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15 pages, 2340 KiB  
Article
Stress-Associated and Growth-Dependent Mutagenesis Are Divergently Regulated by c-di-AMP Levels in Bacillus subtilis
by Karen Abundiz-Yañez, Hilda C. Leyva-Sánchez, Eduardo A. Robleto and Mario Pedraza-Reyes
Int. J. Mol. Sci. 2023, 24(1), 455; https://doi.org/10.3390/ijms24010455 - 27 Dec 2022
Cited by 2 | Viewed by 2038
Abstract
A previous proteomic study uncovered a relationship between nutritional stress and fluctuations in levels of diadenylate cyclases (DACs) and other proteins that regulate DAC activity, degrade, or interact with c-di-AMP, suggesting a possible role of this second messenger in B. subtilis stress-associated mutagenesis [...] Read more.
A previous proteomic study uncovered a relationship between nutritional stress and fluctuations in levels of diadenylate cyclases (DACs) and other proteins that regulate DAC activity, degrade, or interact with c-di-AMP, suggesting a possible role of this second messenger in B. subtilis stress-associated mutagenesis (SAM). Here, we investigated a possible role of c-di-AMP in SAM and growth-associated mutagenesis (GAM). Our results showed that in growing cells of B. subtilis YB955 (hisC952, metB25 and leuC427), the DACs CdaA and DisA, which play crucial roles in cell wall homeostasis and chromosomal fidelity, respectively, counteracted spontaneous and Mitomycin-C-induced mutagenesis. However, experiments in which hydrogen peroxide was used to induce mutations showed that single deficiencies in DACs caused opposite effects compared to each other. In contrast, in the stationary-phase, DACs promoted mutations in conditions of nutritional stress. These results tracked with intracellular levels of c-di-AMP, which are significantly lower in cdaA- and disA-deficient strains. The restoration of DAC-deficient strains with single functional copies of the cdaA and/or disA returned SAM and GAM levels to those observed in the parental strain. Taken together, these results reveal a role for c-di-AMP in promoting genetic diversity in growth-limiting conditions in B. subtilis. Finally, we postulate that this novel function of c-di-AMP can be exerted through proteins that possess binding domains for this second messenger and play roles in DNA repair, ion transport, transcriptional regulation, as well as oxidative stress protection. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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15 pages, 2462 KiB  
Article
Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage
by Dhana G. Gorasia, Christine A. Seers, Jacqueline E. Heath, Michelle D. Glew, Hamid Soleimaninejad, Catherine A. Butler, Mark J. McBride, Paul D. Veith and Eric C. Reynolds
Int. J. Mol. Sci. 2022, 23(10), 5681; https://doi.org/10.3390/ijms23105681 - 19 May 2022
Cited by 7 | Viewed by 1980
Abstract
The Bacteroidetes type IX secretion system (T9SS) consists of at least 20 components that translocate proteins with type A or type B C-terminal domain (CTD) signals across the outer membrane (OM). While type A CTD proteins are anchored to the cell surface via [...] Read more.
The Bacteroidetes type IX secretion system (T9SS) consists of at least 20 components that translocate proteins with type A or type B C-terminal domain (CTD) signals across the outer membrane (OM). While type A CTD proteins are anchored to the cell surface via covalent linkage to the anionic lipopolysaccharide, it is still unclear how type B CTD proteins are anchored to the cell surface. Moreover, very little is known about the PorE and PorP components of the T9SS. In this study, for the first time, we identified a complex comprising the OM β-barrel protein PorP, the OM-associated periplasmic protein PorE and the type B CTD protein PG1035. Cross-linking studies supported direct interactions between PorE-PorP and PorP-PG1035. Furthermore, we show that the formation of the PorE-PorP-PG1035 complex was independent of PorU and PorV. Additionally, the Flavobacterium johnsoniae PorP-like protein, SprF, was found bound to the major gliding motility adhesin, SprB, which is also a type B CTD protein. Together, these results suggest that type B-CTD proteins may anchor to the cell surface by binding to their respective PorP-like proteins. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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15 pages, 3248 KiB  
Article
The Longitudinal Dividing Bacterium Candidatus Thiosymbion Oneisti Has a Natural Temperature-Sensitive FtsZ Protein with Low GTPase Activity
by Jinglan Wang, Silvia Bulgheresi and Tanneke den Blaauwen
Int. J. Mol. Sci. 2022, 23(6), 3016; https://doi.org/10.3390/ijms23063016 - 10 Mar 2022
Viewed by 2242
Abstract
FtsZ, the bacterial tubulin-homolog, plays a central role in cell division and polymerizes into a ring-like structure at midcell to coordinate other cell division proteins. The rod-shaped gamma-proteobacterium Candidatus Thiosymbion oneisti has a medial discontinuous ellipsoidal “Z-ring.” Ca. T. oneisti FtsZ shows temperature-sensitive [...] Read more.
FtsZ, the bacterial tubulin-homolog, plays a central role in cell division and polymerizes into a ring-like structure at midcell to coordinate other cell division proteins. The rod-shaped gamma-proteobacterium Candidatus Thiosymbion oneisti has a medial discontinuous ellipsoidal “Z-ring.” Ca. T. oneisti FtsZ shows temperature-sensitive characteristics when it is expressed in Escherichia coli, where it localizes at midcell. The overexpression of Ca. T. oneisti FtsZ interferes with cell division and results in filamentous cells. In addition, it forms ring- and barrel-like structures independently of E. coli FtsZ, which suggests that the difference in shape and size of the Ca. T. oneisti FtsZ ring is likely the result of its interaction with Z-ring organizing proteins. Similar to some temperature-sensitive alleles of E. coli FtsZ, Ca. T. oneisti FtsZ has a weak GTPase and does not polymerize in vitro. The temperature sensitivity of Ca. Thiosymbion oneisti FtsZ is likely an adaptation to the preferred temperature of less than 30 °C of its host, the nematode Laxus oneistus. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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16 pages, 3922 KiB  
Article
The Escherichia coli Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
by Elisa Consoli, Joen Luirink and Tanneke den Blaauwen
Int. J. Mol. Sci. 2021, 22(22), 12101; https://doi.org/10.3390/ijms222212101 - 09 Nov 2021
Cited by 6 | Viewed by 2453
Abstract
The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In Escherichia coli, it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E). Using [...] Read more.
The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In Escherichia coli, it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E). Using BAM-specific antibodies, in E. coli cells, the complex is shown to localize in the lateral wall in foci. The machinery was shown to be enriched at midcell with specific cell cycle timing. The inhibition of septation by aztreonam did not alter the BAM midcell localization substantially. Furthermore, the absence of late cell division proteins at midcell did not impact BAM timing or localization. These results imply that the BAM enrichment at the site of constriction does not require an active cell division machinery. Expression of the Tre1 toxin, which impairs the FtsZ filamentation and therefore midcell localization, resulted in the complete loss of BAM midcell enrichment. A similar effect was observed for YidC, which is involved in the membrane insertion of cell division proteins in the inner membrane. The presence of the Z-ring is needed for preseptal peptidoglycan (PG) synthesis. As BAM was shown to be embedded in the PG layer, it is possible that BAM is inserted preferentially simultaneously with de novo PG synthesis to facilitate the insertion of OMPs in the newly synthesized outer membrane. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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Review

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37 pages, 9595 KiB  
Review
An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome
by Mohamed Attaibi and Tanneke den Blaauwen
Int. J. Mol. Sci. 2022, 23(7), 3537; https://doi.org/10.3390/ijms23073537 - 24 Mar 2022
Cited by 12 | Viewed by 3462
Abstract
The synthesis of a peptidoglycan septum is a fundamental part of bacterial fission and is driven by a multiprotein dynamic complex called the divisome. FtsW and FtsI are essential proteins that synthesize the peptidoglycan septum and are controlled by the regulatory FtsBLQ subcomplex [...] Read more.
The synthesis of a peptidoglycan septum is a fundamental part of bacterial fission and is driven by a multiprotein dynamic complex called the divisome. FtsW and FtsI are essential proteins that synthesize the peptidoglycan septum and are controlled by the regulatory FtsBLQ subcomplex and the activator FtsN. However, their mode of regulation has not yet been uncovered in detail. Understanding this process in detail may enable the development of new compounds to combat the rise in antibiotic resistance. In this review, recent data on the regulation of septal peptidoglycan synthesis is summarized and discussed. Based on structural models and the collected data, multiple putative interactions within FtsWI and with regulators are uncovered. This elaborates on and supports an earlier proposed model that describes active and inactive conformations of the septal peptidoglycan synthesis complex that are stabilized by these interactions. Furthermore, a new model on the spatial organization of the newly synthesized peptidoglycan and the synthesis complex is presented. Overall, the updated model proposes a balance between several allosteric interactions that determine the state of septal peptidoglycan synthesis. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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23 pages, 6987 KiB  
Review
A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria
by Chris L. B. Graham, Hector Newman, Francesca N. Gillett, Katie Smart, Nicholas Briggs, Manuel Banzhaf and David I. Roper
Int. J. Mol. Sci. 2021, 22(23), 12831; https://doi.org/10.3390/ijms222312831 - 27 Nov 2021
Cited by 12 | Viewed by 4401
Abstract
Bacteria must maintain the ability to modify and repair the peptidoglycan layer without jeopardising its essential functions in cell shape, cellular integrity and intermolecular interactions. A range of new experimental techniques is bringing an advanced understanding of how bacteria regulate and achieve peptidoglycan [...] Read more.
Bacteria must maintain the ability to modify and repair the peptidoglycan layer without jeopardising its essential functions in cell shape, cellular integrity and intermolecular interactions. A range of new experimental techniques is bringing an advanced understanding of how bacteria regulate and achieve peptidoglycan synthesis, particularly in respect of the central role played by complexes of Sporulation, Elongation or Division (SEDs) and class B penicillin-binding proteins required for cell division, growth and shape. In this review we highlight relationships implicated by a bioinformatic approach between the outer membrane, cytoskeletal components, periplasmic control proteins, and cell elongation/division proteins to provide further perspective on the interactions of these cell division, growth and shape complexes. We detail the network of protein interactions that assist in the formation of peptidoglycan and highlight the increasingly dynamic and connected set of protein machinery and macrostructures that assist in creating the cell envelope layers in Gram-negative bacteria. Full article
(This article belongs to the Special Issue Bacterial Cell Envelope Biosynthesis)
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