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Evolution can tinker with multi-protein machines and replace them with simpler single-protein systems performing equivalent functions in an equally efficient manner. It is unclear how, on a molecular level, such simplification can arise. With ancestral reconstruction and biochemical analysis, we have traced the evolution of bacterial small heat shock proteins (sHsp), which help to refold proteins from aggregates using either two proteins with different functions (IbpA and IbpB) or a secondarily single sHsp that performs both functions in an equally efficient way. Secondarily single sHsp evolved from IbpA, an ancestor specialized in strong substrate binding. Evolution of an intermolecular binding site drove the alteration of substrate binding properties, as well as the formation of higher-order oligomers. Upon two mutations in the α-crystallin domain, secondarily single sHsp interacts with aggregated substrates less tightly. Paradoxically, less efficient binding positively influences the ability of sHsp to stimulate substrate refolding, since the dissociation of sHps from aggregates is required to initiate Hsp70-Hsp100-dependent substrate refolding. After the loss of a partner, IbpA took over its role in facilitating the sHsp dissociation from an aggregate by weakening the interaction with the substrate, which became beneficial for the refolding process. We show that the same two amino acids introduced in modern-day systems define whether the IbpA acts as a single sHsp or obligatorily cooperates with an IbpB partner. Our discoveries illuminate how one sequence has evolved to encode functions previously performed by two distinct proteins.
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Autorzy (7)
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Piotr Karaś dr
- University of Gdańsk
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Klaudia Kochanowicz mgr
- University of Gdańsk
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Marcin Pitek mgr
- University of Gdańsk
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Igor Obuchowski
- University of Gdańsk
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Bartłomiej Tomiczek dr inż
- University of Gdańsk
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Krzysztof Liberek prof. dr hab.
- University of Gdańsk
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Pełna treść
- Wersja publikacji
- Accepted albo Published Version
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.7554/eLife.89813
- Licencja
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otwiera się w nowej karcie
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Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuły w czasopismach
- Opublikowano w:
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eLife
strony 1 - 21,
ISSN: 2050-084X - Język:
- angielski
- Rok wydania:
- 2023
- Opis bibliograficzny:
- Karaś P., Kochanowicz K., Pitek M., Domański P., Obuchowski I., Tomiczek B., Liberek K.: Evolution towards simplicity in bacterial small heat shock protein system// eLife -, (2023), s.1-21
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.7554/elife.89813
- Źródła finansowania:
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- Narodowe Centrum Nauki (OPUS 17 2019/33/B/NZ1/00352) Narodowe Centrum Nauki (OPUS 21 2021/41/B/NZ8/02835)
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 11 razy
Publikacje, które mogą cię zainteresować
Karaś P., Kochanowicz K., Pitek M., Domański P., Obuchowski I., Tomiczek B., Liberek K.: Evolution towards simplicity in bacterial small heat shock protein system// eLife -, (2023), s.1-21
- P. Karaś,
- K. Kochanowicz,
- M. Pitek
- + 4 autorów
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- F. Cantini,
- Ł. Nierzwicki
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Characterization of a single-stranded DNA-binding-like Protein from Nanoarchaeum equitans - a nucleic acid binding protein with broad substrate specificity
- M. Olszewski,
- J. Balsewicz,
- M. Nowak
- + 5 autorów