التفاصيل البيبلوغرافية
| العنوان: |
Bacillus subtilis Matrix Protein TasA is Interfacially Active, but BslA Dominates Interfacial Film Properties |
| المؤلفون: |
Ryan J. Morris, Natalie C. Bamford, Keith M. Bromley, Elliot Erskine, Nicola R. Stanley-Wall, Cait E. MacPhee |
| سنة النشر: |
2024 |
| المجموعة: |
Smithsonian Institution: Figshare |
| مصطلحات موضوعية: |
Biophysics, Biochemistry, Inorganic Chemistry, Astronomical and Space Sciences not elsewhere classified, Biological Sciences not elsewhere classified, Physical Sciences not elsewhere classified, strand secondary structure, stable film integral, stable elastic film, induced restructuring similar, forms nonelastic films, bacillus subtilis serves, subtilis biofilm hydrophobicity, protective extracellular matrix, interfacial protein film, elastic protein film, biofilm matrix formation, interface may result, bsla film formation, tasa rapidly reaches, model wherein surface, potentially preventing bsla, tasa undergoes interface, bsla exhibits surface, potentially surface, multiple matrix, biofilm research, rapidly relax, model organism, interface space |
| الوصف: |
Microbial growth often occurs within multicellular communities called biofilms, where cells are enveloped by a protective extracellular matrix. Bacillus subtilis serves as a model organism for biofilm research and produces two crucial secreted proteins, BslA and TasA, vital for biofilm matrix formation. BslA exhibits surface-active properties, spontaneously self-assembling at hydrophobic/hydrophilic interfaces to form an elastic protein film, which renders B. subtilis biofilm surfaces water-repellent. TasA is traditionally considered a fiber-forming protein with multiple matrix-related functions. In our current study, we investigate whether TasA also possesses interfacial properties and whether it has any impact on BslA’s ability to form an interfacial protein film. Our research demonstrates that TasA indeed exhibits interfacial activity, partitioning to hydrophobic/hydrophilic interfaces, stabilizing emulsions, and forming an interfacial protein film. Interestingly, TasA undergoes interface-induced restructuring similar to BslA, showing an increase in β-strand secondary structure. Unlike BslA, TasA rapidly reaches the interface and forms nonelastic films that rapidly relax under pressure. Through mixed protein pendant drop experiments, we assess the influence of TasA on BslA film formation, revealing that TasA and other surface-active molecules can compete for interface space, potentially preventing BslA from forming a stable elastic film. This raises a critical question: how does BslA self-assemble to form the hydrophobic “raincoat” observed in biofilms in the presence of other potentially surface-active species? We propose a model wherein surface-active molecules, including TasA, initially compete with BslA for interface space. However, under lateral compression or pressure, BslA retains its position, expelling other molecules into the bulk. This resilience at the interface may result from structural rearrangements and lateral interactions between BslA subunits. This combined mechanism likely explains BslA’s ... |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
unknown |
| Relation: |
https://figshare.com/articles/journal_contribution/Bacillus_subtilis_Matrix_Protein_TasA_is_Interfacially_Active_but_BslA_Dominates_Interfacial_Film_Properties/25217791 |
| DOI: |
10.1021/acs.langmuir.3c03163.s001 |
| الاتاحة: |
https://doi.org/10.1021/acs.langmuir.3c03163.s001 |
| Rights: |
CC BY-NC 4.0 |
| رقم الانضمام: |
edsbas.14B89327 |
| قاعدة البيانات: |
BASE |