Thermo-resistant intrinsically disordered proteins are efficient 20S proteasome substrates.
Based on software prediction, intrinsically disordered proteins (IDPs) are widely represented in animal cells where they play important instructive roles. Despite the predictive power of the available software programs we nevertheless need simple experimental tools to validate the predictions. IDPs were reported to be preferentially thermo-resistant and also are susceptible to degradation by the 20S proteasome. Analysis of a set of proteins revealed that thermo-resistant proteins are preferred 20S proteasome substrates. Positive correlations are evident between the percent of protein disorder and the level of thermal stability and 20S proteasomal susceptibility. The data obtained from these two assays do not fully overlap but in combination provide a more reliable experimental IDP definition. The correlation was more significant when the IUPred was used as the IDPs predicting software. We demonstrate in this work a simple experimental strategy to improve IDPs identification.
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Peter
P
Tsvetkov
Nadav
N
Myers
Oren
O
Moscovitz
Michal
M
Sharon
Jaime
J
Prilusky
Yosef
Y
Shaul
D006367:HeLa Cells; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D059748:Proteolysis; D013379:Substrate Specificity; D013696:Temperature
D046912:Multiprotein Complexes; D011506:Proteins; D046988:Proteasome Endopeptidase Complex