Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein
Bacterial S1 protein is a functionally important ribosomal protein. It is a part of the 30S ribosomal subunit and is also able to interact with mRNA and tmRNA. An important feature of the S1 protein family is a strong tendency towards aggregation. To study the amyloidogenic properties of S1, we isol...
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MDPI AG
2021-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/14/7291 |
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| author | Sergei Y. Grishin Ulyana F. Dzhus Anatoly S. Glukhov Olga M. Selivanova Alexey K. Surin Oxana V. Galzitskaya |
| author_facet | Sergei Y. Grishin Ulyana F. Dzhus Anatoly S. Glukhov Olga M. Selivanova Alexey K. Surin Oxana V. Galzitskaya |
| author_sort | Sergei Y. Grishin |
| collection | DOAJ |
| description | Bacterial S1 protein is a functionally important ribosomal protein. It is a part of the 30S ribosomal subunit and is also able to interact with mRNA and tmRNA. An important feature of the S1 protein family is a strong tendency towards aggregation. To study the amyloidogenic properties of S1, we isolated and purified the recombinant ribosomal S1 protein of <i>Pseudomonas aeruginosa</i>. Using the FoldAmyloid, Waltz, Pasta 2.0, and AGGRESCAN programs, amyloidogenic regions of the protein were predicted, which play a key role in its aggregation. The method of limited proteolysis in combination with high performance liquid chromatography and mass spectrometric analysis of the products, made it possible to identify regions of the S1 protein from <i>P. aeruginosa</i> that are protected from the action of proteinase K, trypsin, and chymotrypsin. Sequences of theoretically predicted and experimentally identified amyloidogenic regions were used to synthesize four peptides, three of which demonstrated the ability to form amyloid-like fibrils, as shown by electron microscopy and fluorescence spectroscopy. The identified amyloidogenic sites can further serve as a basis for the development of new antibacterial peptides against the pathogenic microorganism <i>P. aeruginosa</i>. |
| first_indexed | 2024-03-10T09:37:45Z |
| format | Article |
| id | doaj.art-e5b1adebacbb4844b23b5cfef42c6ade |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T09:37:45Z |
| publishDate | 2021-07-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-e5b1adebacbb4844b23b5cfef42c6ade2023-11-22T03:56:08ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-07-012214729110.3390/ijms22147291Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 ProteinSergei Y. Grishin0Ulyana F. Dzhus1Anatoly S. Glukhov2Olga M. Selivanova3Alexey K. Surin4Oxana V. Galzitskaya5Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaBacterial S1 protein is a functionally important ribosomal protein. It is a part of the 30S ribosomal subunit and is also able to interact with mRNA and tmRNA. An important feature of the S1 protein family is a strong tendency towards aggregation. To study the amyloidogenic properties of S1, we isolated and purified the recombinant ribosomal S1 protein of <i>Pseudomonas aeruginosa</i>. Using the FoldAmyloid, Waltz, Pasta 2.0, and AGGRESCAN programs, amyloidogenic regions of the protein were predicted, which play a key role in its aggregation. The method of limited proteolysis in combination with high performance liquid chromatography and mass spectrometric analysis of the products, made it possible to identify regions of the S1 protein from <i>P. aeruginosa</i> that are protected from the action of proteinase K, trypsin, and chymotrypsin. Sequences of theoretically predicted and experimentally identified amyloidogenic regions were used to synthesize four peptides, three of which demonstrated the ability to form amyloid-like fibrils, as shown by electron microscopy and fluorescence spectroscopy. The identified amyloidogenic sites can further serve as a basis for the development of new antibacterial peptides against the pathogenic microorganism <i>P. aeruginosa</i>.https://www.mdpi.com/1422-0067/22/14/7291ribosomal S1 proteinsamyloidogenic regionstoxicityantibacterial peptidesamyloidmass spectrometry |
| spellingShingle | Sergei Y. Grishin Ulyana F. Dzhus Anatoly S. Glukhov Olga M. Selivanova Alexey K. Surin Oxana V. Galzitskaya Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein International Journal of Molecular Sciences ribosomal S1 proteins amyloidogenic regions toxicity antibacterial peptides amyloid mass spectrometry |
| title | Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein |
| title_full | Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein |
| title_fullStr | Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein |
| title_full_unstemmed | Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein |
| title_short | Identification of Amyloidogenic Regions in <i>Pseudomonas aeruginosa</i> Ribosomal S1 Protein |
| title_sort | identification of amyloidogenic regions in i pseudomonas aeruginosa i ribosomal s1 protein |
| topic | ribosomal S1 proteins amyloidogenic regions toxicity antibacterial peptides amyloid mass spectrometry |
| url | https://www.mdpi.com/1422-0067/22/14/7291 |
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