Year 2024

• Functional similarities and differences among subunits of the nascent polypeptide-associated complex (NAC) of Saccharomyces cerevisiae

  Publication

  • B. A. Schilke
  • T. Ziegelhoffer
  • P. Domański
  • J. Marszalek
  • B. Tomiczek
  • E. Craig

  - CELL STRESS & CHAPERONES - Year 2024

  Protein factors bind ribosomes near the tunnel exit, facilitating protein trafficking and folding. In eukaryotes, the heterodimeric nascent polypeptide-associated complex (NAC) is the most abundant - equimolar to ribosomes. Saccharomyces cerevisiae has a minor β-type subunit (Nacβ2) in addition to abundant Nacβ1, and therefore two NAC heterodimers, α/β1 and α/β12. The additional beta NAC gene arose at the time of the whole genome...

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Year 2023

• 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

  Publication

  • P. Karaś
  • K. Kochanowicz
  • M. Pitek
  • P. Domański
  • I. Obuchowski
  • B. Tomiczek
  • K. Liberek

  - eLife - Year 2023

  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...

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