Publications by authors named "Przemyslaw Domanski"
Article Synopsis
- Protein factors, specifically the nascent polypeptide-associated complex (NAC), bind to ribosomes to aid in protein trafficking and folding in eukaryotes, particularly in yeast like Saccharomyces cerevisiae.
- The NAC consists of two beta subunits, Nacβ1 and a minor Nacβ2, with Nacβ2 playing a crucial role in regulating the messenger RNA (mRNA) of ribosomal protein Rpl4 during translation by interacting with the CCR4-Not complex.
- Research indicates that specific Nacβ2 residues are crucial for its interaction with Caf130, and modifying these residues can significantly impact cell growth, suggesting that the positioning of Nacβ2 is vital for effective mRNA degradation
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.
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