The group's research indicates that the protein in the fungal genus Neurospora they studied, frequency, performs better when the genetic code specifying it has non-optimal codon usage, as is normally found. However, when the genetic code is deliberately altered so that codon usage is optimized, clock function is lost. The reason for this is that non-optimal codon usage slows translation of the genetic code into protein, allotting the frequency protein the necessary time to achieve its optimal protein structure. The team's results also demonstrate that genetic codons do more than simply determine the amino acid sequence of a protein as previously thought: They also affect how much protein can be made as well as the functional quality of that protein.
"We found that less is more, in many cases," Liu said.
Because many genetic diseases are the result of improperly functioning proteins, Sachs says knowledge about how proteins are made and why they have impaired functions is critical to understanding almost all diseases.
"Understanding gene expression is crucial for understanding cancer and other diseases, because ultimately many of these processes involve either mutations of genes or altered expression of genes," said Sachs, who was asked by Liu to help on the research because of his translational expertise in Neurospora.
In addition to Liu and Sachs, the paper's authors include Mian Zhou , Jinhu Guo , Joonseok Cha and Michael Chae , all from the D
|SOURCE Texas A&M University|
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