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FtsZ filament capping by MciZ, a developmental regulator of bacterial division

Bisson-Filho, Alexandre W. ; Discola, Karen F. ; Castellen, Patrícia ; [et al.]

Proceedings of the National Academy of Sciences ; 2015

In: Proceedings of the National Academy of Sciences Vol. 112, No. 17 ( 2015-04-28)

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In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 112, No. 17 ( 2015-04-28)

Abstract: Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. Here we investigate the mechanism by which the Bacillus subtilis cell-division inhibitor, MciZ (mother cell inhibitor of FtsZ), blocks assembly of FtsZ. The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. The findings demonstrate an unanticipated capping-based regulatory mechanism for FtsZ.

Type of Medium: Online Resource

ISSN: 0027-8424 , 1091-6490

URL: Article

DOI: 10.1073/pnas.1414242112

RVK:

TA 1000

RVK:

WA 15000

Language: English

Publisher: Proceedings of the National Academy of Sciences

Publication Date: 2015

detail.hit.zdb_id: 209104-5

detail.hit.zdb_id: 1461794-8

SSG: 11

SSG: 12

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Genetic and Biochemical Characterization of the MinC-FtsZ Interaction in Bacillus subtilis

Blasios, Valdir ; Bisson-Filho, Alexandre W. ; Castellen, Patricia ; [et al.]

Public Library of Science (PLoS) ; 2013

In: PLoS ONE Vol. 8, No. 4 ( 2013-4-5), p. e60690-

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In: PLoS ONE, Public Library of Science (PLoS), Vol. 8, No. 4 ( 2013-4-5), p. e60690-

Type of Medium: Online Resource

ISSN: 1932-6203

URL: Article

DOI: 10.1371/journal.pone.0060690

DOI: 10.1371/journal.pone.0060690.g001

DOI: 10.1371/journal.pone.0060690.g002

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DOI: 10.1371/journal.pone.0060690.t001

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DOI: 10.1371/journal.pone.0060690.s001

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DOI: 10.1371/journal.pone.0060690.s012

DOI: 10.1371/journal.pone.0060690.s013

DOI: 10.1371/journal.pone.0060690.s014

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2013

detail.hit.zdb_id: 2267670-3

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DivIVA-Mediated Polar Localization of ComN, a Posttranscriptional Regulator of Bacillus subtilis

dos Santos, Valquiria Tiago ; Bisson-Filho, Alexandre W. ; Gueiros-Filho, Frederico J.

American Society for Microbiology ; 2012

In: Journal of Bacteriology Vol. 194, No. 14 ( 2012-07-15), p. 3661-3669

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In: Journal of Bacteriology, American Society for Microbiology, Vol. 194, No. 14 ( 2012-07-15), p. 3661-3669

Abstract: ComN (YrzD) is a small, 98-amino-acid protein recently shown to be involved in the posttranscriptional control of the late competence comE operon in Bacillus subtilis . We show here that ComN localizes to the division site and cell poles in a DivIVA-dependent fashion. Yeast two-hybrid and glutathione S -transferase pulldown experiments showed that ComN interacts directly with DivIVA. ComN is not essential for the polar assembly of the core competence DNA uptake machinery. Nevertheless, polar localization of ComN should play some role in competence acquisition because delocalization of ComN leads to a small reduction in competence efficiency. We found that ComN promotes the accumulation of its target comE mRNA to septal and polar sites. Thus, we speculate that localized translation of ComE proteins may be required for efficient competence development. Our results underscore the versatility of DivIVA as a promoter of the differentiation of bacterial poles and demonstrate that the repertoire of polarly localized molecules in B. subtilis is broad, including a regulator of gene expression and its target mRNA. Moreover, our findings suggest that mRNA localization may play a role in the subcellular organization of bacteria.

Type of Medium: Online Resource

ISSN: 0021-9193 , 1098-5530

URL: Article

DOI: 10.1128/JB.05879-11

Language: English

Publisher: American Society for Microbiology

Publication Date: 2012

detail.hit.zdb_id: 1481988-0

SSG: 12

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Treadmilling by FtsZ filaments drives peptidoglycan synthesis and bacterial cell division

Bisson-Filho, Alexandre W. ; Hsu, Yen-Pang ; Squyres, Georgia R. ; [et al.]

American Association for the Advancement of Science (AAAS) ; 2017

In: Science Vol. 355, No. 6326 ( 2017-02-17), p. 739-743

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In: Science, American Association for the Advancement of Science (AAAS), Vol. 355, No. 6326 ( 2017-02-17), p. 739-743

Abstract: The mechanism by which bacteria divide is not well understood. Cell division is mediated by filaments of FtsZ and FtsA (FtsAZ) that recruit septal peptidoglycan-synthesizing enzymes to the division site. To understand how these components coordinate to divide cells, we visualized their movements relative to the dynamics of cell wall synthesis during cytokinesis. We found that the division septum was built at discrete sites that moved around the division plane. FtsAZ filaments treadmilled circumferentially around the division ring and drove the motions of the peptidoglycan-synthesizing enzymes. The FtsZ treadmilling rate controlled both the rate of peptidoglycan synthesis and cell division. Thus, FtsZ treadmilling guides the progressive insertion of new cell wall by building increasingly smaller concentric rings of peptidoglycan to divide the cell.

Type of Medium: Online Resource

ISSN: 0036-8075 , 1095-9203

URL: Article

DOI: 10.1126/science.aak9973

RVK:

TA 1000

RVK:

WA 15000

Language: English

Publisher: American Association for the Advancement of Science (AAAS)

Publication Date: 2017

detail.hit.zdb_id: 128410-1

detail.hit.zdb_id: 2066996-3

detail.hit.zdb_id: 2060783-0

SSG: 11

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Bacterial killing via a type IV secretion system

Souza, Diorge P. ; Oka, Gabriel U. ; Alvarez-Martinez, Cristina E. ; [et al.]

Springer Science and Business Media LLC ; 2015

In: Nature Communications Vol. 6, No. 1 ( 2015-03-06)

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In: Nature Communications, Springer Science and Business Media LLC, Vol. 6, No. 1 ( 2015-03-06)

Type of Medium: Online Resource

ISSN: 2041-1723

URL: Article

DOI: 10.1038/ncomms7453

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2015

detail.hit.zdb_id: 2553671-0

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A survey-based analysis of the academic job market

Fernandes, Jason D ; Sarabipour, Sarvenaz ; Smith, Christopher T ; [et al.]

eLife Sciences Publications, Ltd ; 2020

In: eLife Vol. 9 ( 2020-06-12)

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In: eLife, eLife Sciences Publications, Ltd, Vol. 9 ( 2020-06-12)

Abstract: Many postdoctoral researchers apply for faculty positions knowing relatively little about the hiring process or what is needed to secure a job offer. To address this lack of knowledge about the hiring process we conducted a survey of applicants for faculty positions: the survey ran between May 2018 and May 2019, and received 317 responses. We analyzed the responses to explore the interplay between various scholarly metrics and hiring outcomes. We concluded that, above a certain threshold, the benchmarks traditionally used to measure research success – including funding, number of publications or journals published in – were unable to completely differentiate applicants with and without job offers. Respondents also reported that the hiring process was unnecessarily stressful, time-consuming, and lacking in feedback, irrespective of outcome. Our findings suggest that there is considerable scope to improve the transparency of the hiring process.

Type of Medium: Online Resource

ISSN: 2050-084X

URL: Article

DOI: 10.7554/eLife.54097

Language: English

Publisher: eLife Sciences Publications, Ltd

Publication Date: 2020

detail.hit.zdb_id: 2687154-3

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Author response image 1.

Hussain, Saman ; Wivagg, Carl N ; Szwedziak, Piotr ; [et al.]

eLife Sciences Publications, Ltd ; 2018

In: eLife Vol. 7 ( 2018-02-22)

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In: eLife, eLife Sciences Publications, Ltd, Vol. 7 ( 2018-02-22)

Abstract: Many bacteria are surrounded by both a cell membrane and a cell wall – a rigid outer covering made of sugars and short protein chains. The cell wall often determines which of a variety of shapes – such as rods or spheres – the bacteria grow into. One protein required to form the rod shape is called MreB. This protein forms filaments that bind to the bacteria’s cell membrane and associate with the enzymes that build the cell wall. Together, these filament-enzyme complexes rotate around the cell to build and reinforce the cell wall in a hoop-like manner. But how do the MreB filaments know how to move around the circumference of the rod, instead of moving in any other direction? Using a technique called total internal reflection microscopy to study how MreB filaments move across bacteria cells, Hussain, Wivagg et al. show that the filaments sense the shape of a bacterium by orienting along the direction of greatest curvature. As a result, the filaments in rod-shaped cells orient and move around the rod, while in spherical bacteria they move in all directions. However, spherical bacteria can regenerate into rods from small surface ‘bulges’. The MreB filaments in the bulges move in an oriented way, helping them to generate the rod shape. Hussain, Wivagg et al. also found that forcing cells that lack a cell wall into a rod shape caused the MreB filaments bound to the cell membrane to orient and circle around the rod. This shows that the organization of the filaments is sufficient to shape the cell wall. In the future, determining what factors control the activity of the MreB filaments and the enzymes they associate with might reveal new targets for antibiotics that disrupt the cell wall and so kill the bacteria. This will require higher resolution microscopes to be used to examine the cell wall in more detail. The activity of all the proteins involved in building cell walls will also need to be extensively characterized.

Type of Medium: Online Resource

ISSN: 2050-084X

URL: Article

DOI: 10.7554/eLife.32471

DOI: 10.7554/eLife.32471.001

DOI: 10.7554/eLife.32471.002

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DOI: 10.7554/eLife.32471.052

DOI: 10.7554/eLife.32471.050

Language: English

Publisher: eLife Sciences Publications, Ltd

Publication Date: 2018

detail.hit.zdb_id: 2687154-3

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Division plane placement in pleomorphic archaea is dynamically coupled to cell shape

Walsh, James C. ; Angstmann, Christopher N. ; Bisson‐Filho, Alexandre W. ; [et al.]

Wiley ; 2019

In: Molecular Microbiology Vol. 112, No. 3 ( 2019-09), p. 785-799

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In: Molecular Microbiology, Wiley, Vol. 112, No. 3 ( 2019-09), p. 785-799

Abstract: One mechanism for achieving accurate placement of the cell division machinery is via Turing patterns, where nonlinear molecular interactions spontaneously produce spatiotemporal concentration gradients. The resulting patterns are dictated by cell shape. For example, the Min system of Escherichia coli shows spatiotemporal oscillation between cell poles, leaving a mid‐cell zone for division. The universality of pattern‐forming mechanisms in divisome placement is currently unclear. We examined the location of the division plane in two pleomorphic archaea, Haloferax volcanii and Haloarcula japonica , and showed that it correlates with the predictions of Turing patterning. Time‐lapse analysis of H. volcanii shows that divisome locations after successive rounds of division are dynamically determined by daughter cell shape. For H. volcanii , we show that the location of DNA does not influence division plane location, ruling out nucleoid occlusion. Triangular cells provide a stringent test for Turing patterning, where there is a bifurcation in division plane orientation. For the two archaea examined, most triangular cells divide as predicted by a Turing mechanism; however, in some cases multiple division planes are observed resulting in cells dividing into three viable progeny. Our results suggest that the division site placement is consistent with a Turing patterning system in these archaea.

Type of Medium: Online Resource

ISSN: 0950-382X , 1365-2958

URL: Issue

URL: Article

DOI: 10.1111/mmi.v112.3

DOI: 10.1111/mmi.14316

Language: English

Publisher: Wiley

Publication Date: 2019

detail.hit.zdb_id: 1501537-3

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Preprint Highlight: Pressure and curvature control of contact inhibition in epithelia growing under spherical confinement

Bisson-Filho, Alexandre W.

American Society for Cell Biology (ASCB) ; 2022

In: Molecular Biology of the Cell Vol. 33, No. 4 ( 2022-04-01)

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In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 33, No. 4 ( 2022-04-01)

Abstract: All living systems evolved molecular mechanisms to respond to their physical surroundings, such as by tuning cell cycle progression as well as transport of different cargo across intracellular compartments. However, it is difficult to determine if such responses are genetically programmed or purely resultant of physical forces. This study deploys a new confinement device that modulates chamber stiffness, curvature, and compression over epithelial tissue. Compression specifically regulated cell cycle progression, while increasing stiffness changed cell aspect ratio. The authors propose a new independent function of previous cooperative pathways that regulate long-range tissue scales (β-catenin) and local spatial changes (YAP/TAZ). This work represents a methodological advance in creating specific physical cues while measuring cellular processes, enabling many future studies combining other chemical and genetic perturbations.

Type of Medium: Online Resource

ISSN: 1059-1524 , 1939-4586

URL: Article

DOI: 10.1091/mbc.P22-02-1002

Language: English

Publisher: American Society for Cell Biology (ASCB)

Publication Date: 2022

detail.hit.zdb_id: 1474922-1

SSG: 12

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Haloferax volcanii Immersed Liquid Biofilms Develop Independently of Known Biofilm Machineries and Exhibit Rapid Honeycomb Pattern Formation

Schiller, Heather ; Schulze, Stefan ; Mutan, Zuha ; [et al.]

American Society for Microbiology ; 2020

In: mSphere Vol. 5, No. 6 ( 2020-12-23)

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In: mSphere, American Society for Microbiology, Vol. 5, No. 6 ( 2020-12-23)

Abstract: The ability to form biofilms is shared by many microorganisms, including archaea. Cells in a biofilm are encased in extracellular polymeric substances that typically include polysaccharides, proteins, and extracellular DNA, conferring protection while providing a structure that allows for optimal nutrient flow. In many bacteria, flagella and evolutionarily conserved type IV pili are required for the formation of biofilms on solid surfaces or floating at the air-liquid interface of liquid media. Similarly, in many archaea it has been demonstrated that type IV pili and, in a subset of these species, archaella are required for biofilm formation on solid surfaces. Additionally, in the model archaeon Haloferax volcanii , chemotaxis and AglB-dependent glycosylation play important roles in this process. H. volcanii also forms immersed biofilms in liquid cultures poured into petri dishes. This study reveals that mutants of this haloarchaeon that interfere with the biosynthesis of type IV pili or archaella, as well as a chemotaxis-targeting transposon and aglB deletion mutants, lack obvious defects in biofilms formed in liquid cultures. Strikingly, we have observed that these liquid-based biofilms are capable of rearrangement into honeycomb-like patterns that rapidly form upon removal of the petri dish lid, a phenomenon that is not dependent on changes in light or oxygen concentration but can be induced by controlled reduction of humidity. Taken together, this study demonstrates that H. volcanii requires novel, unidentified strategies for immersed liquid biofilm formation and also exhibits rapid structural rearrangements. IMPORTANCE This first molecular biological study of archaeal immersed liquid biofilms advances our basic biological understanding of the model archaeon Haloferax volcanii . Data gleaned from this study also provide an invaluable foundation for future studies to uncover components required for immersed liquid biofilms in this haloarchaeon and also potentially for liquid biofilm formation in general, which is poorly understood compared to the formation of biofilms on surfaces. Moreover, this first description of rapid honeycomb pattern formation is likely to yield novel insights into the underlying structural architecture of extracellular polymeric substances and cells within immersed liquid biofilms.

Type of Medium: Online Resource

ISSN: 2379-5042

URL: Article

DOI: 10.1128/mSphere.00976-20

Language: English

Publisher: American Society for Microbiology

Publication Date: 2020

detail.hit.zdb_id: 2844248-9

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