Modeling shows how genetic changes that don’t lead to changes in protein sequence can still alter protein function. New modeling shows how synonymous mutations — those that change the DNA sequence of a gene but not the sequence of the encoded protein — can still impact protein production and func
Illustration of a new class of protein misfolding called a non-covalent lasso entanglement that can result from changes to the rate of protein synthesis caused by synonymous mutations. Bottom: structure of a protein showing its native state and misfolded state with non-covalent lasso entanglement. Credit: Yang Jiang, Penn State
The results demonstrate the importance of kinetics — the rate of protein synthesis — in addition to sequence for determining protein structure and function and could have implications in fields such as biopharmaceutics for fine-tuning the activity of synthesized proteins. “We used to use ‘synonymous’ and ‘silent’ interchangeably to describe mutations that don’t change a protein’s sequence because it was thought that they wouldn’t alter the function of the protein,” said Ed O’Brien, professor of chemistry and a member of the Institute for Computational and Data Sciences at Penn State, and one of the leaders of the research team. “But, we’ve known for some time now that not all synonymous mutations are silent.
“In our models, we found a new class of protein misfolding that we call a ‘non-covalent lasso entanglement,’” said Jiang. “Essentially, a portion of the protein forms a closed loop, and one end of the protein incorrectly threads through the loop and gets trapped for long time periods.” These new insights into how the kinetics of protein synthesis can influence protein structure and function could have repercussions in fields ranging from biochemistry to biotechnology and to medicine.
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