Structural changes of TasA in biofilm formation of
            <i>Bacillus subtilis</i>

Diehl, Anne; Roske, Yvette; Ball, Linda; Chowdhury, Anup; Hiller, Matthias; Molière, Noël; Kramer, Regina; Stöppler, Daniel; Worth, Catherine L.; Schlegel, Brigitte; Leidert, Martina; Cremer, Nils; Erdmann, Natalja; López, Daniel; Stephanowitz, Heike; Krause, Eberhard; Rossum, Barth‐Jan van; Schmieder, Peter; Heinemann, Udo; Turgay, Kürşad; Akbey, Ümit; Oschkinat, Hartmut

doi:10.1073/pnas.1718102115

Cited by 98 publications

(131 citation statements)

References 42 publications

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“…In this work, we describe the structural comparison of TasA functional amyloid fibrils from B. subtilis and B. cereus alongside their accessory proteins, TapA and CalY, respectively. These results together with previous studies (20)(21)(22)(23)(24)(25) allow us to establish a mechanistic picture of TasA assembly in both Bacillus species (Fig. 10).…”

Section: Discussionsupporting

confidence: 79%

“…Interestingly, 2D [ 13 C]‐[ 13 C] SSNMR fingerprints for TasA‐bs and TasA‐bc superimpose quite well, indicating that the overall structural fold between the 2 is similar. The crystal structure (24) uncovered TasA globular monomeric form, which consists of a jelly‐roll fold comprising 2 antiparallel β ‐sheets surrounded with 6 short α‐helices and several loops. Fascinating is the idea that TasA‐bs fibrils might, upon assembly, conserve a part of the TasA globular form while adjusting β ‐strands in a cross‐β stacking manner within its amyloid core.…”

Section: Discussionmentioning

confidence: 99%

“…S3C) displays equally limited 1 H dispersion (;1 ppm), also indicating a predominantly unstructured conformation. Such observations are quite interesting because no data have yet been reported for the B. cereus biofilmforming proteins TasA-bc and CalY (in these conditions) in their monomeric form and, therefore, the above characterization suggests drastic differences between B. cereus and B. subtilis, whereby both TasA-bs and TapA show a structured fold and an only partially disordered fold, respectively (24,32).…”

Section: Tasa-bc and Caly Maintain An Unfolded Conformation In Solutionmentioning

confidence: 99%

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Molecular architecture of bacterial amyloids in Bacillus biofilms

Mammeri

Hierrezuelo²,

Tolchard

et al. 2019

FASEB j.

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The formation of biofilms provides structural and adaptive bacterial response to the environment. In Bacillus species, the biofilm extracellular matrix is composed of exopolysaccharides, hydrophobins, and several functional amyloid proteins. We report, using multiscale approaches such as solid‐state NMR (SSNMR), electron microscopy, X‐ray diffraction, dynamic light scattering, attenuated total reflection Fourier transform infrared (FTIR), and immune‐gold labeling, the molecular architecture of B. subtilis and pathogenic B. cereus functional amyloids. SSNMR data reveal that the major amyloid component TasA in its fibrillar amyloid form contain β‐sheet and α‐helical secondary structure, suggesting a nontypical amyloid architecture in B. subtilis. Proteinase K digestion experiments indicate the amyloid moiety is ~100 aa long, and subsequent SSNMR and FTIR signatures for B. subtilis and B. cereus TasA filaments highlight a conserved amyloid fold, albeit with substantial differences in structural polymorphism and secondary structure composition. Structural analysis and coassembly data on the accessory protein TapA in B. subtilis and its counterpart camelysin in B. cereus reveal a catalyzing effect between the functional amyloid proteins and a common structural architecture, suggesting a coassembly in the context of biofilm formation. Our findings highlight nontypical amyloid behavior of these bacterial functional amyloids, underlining structural variations between biofilms even in closely related bacterial species.—El Mammeri, N., Hierrezuelo, J., Tolchard, J., Cámara‐Almirón, J., Caro‐Astorga, J., Álvarez‐Mena, A., Dutour, A., Berbon, M., Shenoy, J., Morvan, E., Grélard, A., Kauffmann, B., Lecomte, S., de Vicente, A., Habenstein, B., Romero, D., Loquet, A. Molecular architecture of bacterial amyloids in Bacillus biofilms. FASEB J. 33, 12146‐12163 (2019). http://www.fasebj.org

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

Section: Tasa-bc and Caly Maintain An Unfolded Conformation In Solutionmentioning

confidence: 99%

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Molecular architecture of bacterial amyloids in Bacillus biofilms

Mammeri

Hierrezuelo²,

Tolchard

et al. 2019

FASEB j.

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“…A previous analysis of the sequence of TapA revealed two conserved fragments (marked red in Figure A): a 37‐residue fragment, TapA 194–230, at the C terminus of the protein, which had no phenotypic effect on biofilms, and an 8‐residue fragment, TapA 50–57, at the N terminus of the protein, which affected the phenotype of the biofilm and was essential for TasA fiber assembly in vitro . Unlike the disordered natures of CsgA and CsgB, TasA is a structured protein, as we have previously shown, and was later corroborated by means of X‐ray diffraction . Nevertheless, despite the important role of TapA in forming TasA fibers, there is no information on its structure.…”

Section: Figurementioning

confidence: 59%

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

et al. 2018

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Biofilms are aggregates of microbial cells that form on surfaces and at interfaces, and are encased in an extracellular matrix. In biofilms made by the soil bacterium Bacillus subtilis, the protein TapA mediates the assembly of the functional amyloid protein TasA into extracellular fibers, and it anchors these fibers to the cell surface. We used circular dichroism and NMR spectroscopy to show that, unlike the structured TasA, TapA is disordered. In addition, TapA is composed of two weakly interacting domains: a disordered C‐terminal domain and a more structured N‐terminal domain. These two domains also exhibited different structural changes in response to changes in external conditions, such as increased temperatures and the presence of lipid vesicles. Although the two TapA domains weakly interacted in solution, their cooperative interaction with lipid vesicles prevented disruption of the vesicles. These findings therefore suggest that the two‐domain composition of TapA is important in its interaction with single or multiple partners in the extracellular matrix in biofilms.

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“…Majority of these reported functional amyloids are from Proteobacteria, Actinobacteria, Firmicutes and Bacteroides but only a few of them have been purified and investigated in depth. Thus major functions proposed for FuBA generalized for all bacterial amyloids are still speculations [3], [11]. Recently, the TasA amyloid protein from Bacillus subtilis was studied by crystal structure as 5OF1 and 5OF2 [12] and in present manuscript, its structure has been used for nucleation studies and interaction of other amyloid proteins.…”

Section: Resultsmentioning

confidence: 92%

In Silico Analysis of Bacterial Functional Amyloids and their Interactions

Mehta¹

2018

IJRASET

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Amyloid proteins have been known to be responsible for many neurodegenerative diseases of mammals including humans. Histopathologically, amyloid fibres are known to be formed due to mis-folds, mutations and other induction events concerned with these proteins in the patients. Once formed, these amyloid proteins have been well reported to undergo nucleation and form fibrous projections that result in cell-death. In living system (microorganisms and higher organisms alike), similar functional amyloid proteins are known to be produced with similar nucleation process. In this report the homologous proteins were created for functional amyloids from Escherichia coli, Bacillus thuringiensis, Bacillus atropheus, Streptococcus pyogenes and Dinoroseobacter shibae. Using the Z-dock server, analysed their interaction with each other. This report will help in understanding the self-folding and nucleation process of the functional amyloids in bacteria and further correlate the functional amyloids of bacteria with pathological amyloids in mammals.

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Structural changes of TasA in biofilm formation of Bacillus subtilis

Cited by 98 publications

References 42 publications

Molecular architecture of bacterial amyloids in Bacillus biofilms

Molecular architecture of bacterial amyloids in Bacillus biofilms

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

In Silico Analysis of Bacterial Functional Amyloids and their Interactions

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