Protein form and function

In a massive undertaking, Whitehead Institute scientists have tested nearly 700 wild yeast strains isolated from diverse environments for the presence of known and unknown prion elements, finding them in one third of all strains. All the prions appear capable of creating diverse new traits, nearly half of which are beneficial.

According to Whitehead Institute researchers, cells take advantage of a biologically ancient compartment to sequester prions, an action that can initially prevent the prions’ phenotypic expression. While in this compartment, less stably heritable prion plaques also mature to a more transmissible state.

Several structurally similar small molecules appear capable of protecting cells from alpha-synuclein toxicity, a hallmark of Parkinson’s disease, according to Whitehead Institute researchers.

Whitehead Institute researchers have developed a new approach for genetics in human cells and used this technique to identify specific genes and proteins required for pathogens.

Whitehead Institute scientists have determined that a protein known as YOD1 plays a critical role in the disposal of misfolded cellular proteins. The researchers identified YOD1’s role by blocking its function, a manipulation that halts the elimination of errant proteins entirely. The finding should help bring greater understanding to this vital but complex cellular process.

Researchers have created an algorithm that meshes existing data to produce a clearer step-by-step flow chart of how cells respond to stimuli. Using this new method, Whitehead Institute and Massachusetts Institute of Technology scientists have analyzed alpha-synuclein toxicity to identify genes and pathways that can affect cell survival. Misfolded copies of the alpha-synuclein protein in brain cells are a hallmark of Parkinson’s disease.