You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Census of Glutamine/Asparagine-Rich Regions: Implications for Their Conserved Function and the Prediction of Novel Prions
Melissa D. Michelitsch and Jonathan S. Weissman
Proceedings of the National Academy of Sciences of the United States of America
Vol. 97, No. 22 (Oct. 24, 2000), pp. 11910-11915
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/123764
Page Count: 6
You can always find the topics here!Topics: Prions, Amino acids, Proteomes, Thermophilic microorganisms, Yeasts, Open reading frames, Aggregation, Mathematical functions, Eukaryotic cells, Cell aggregates
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Glutamine/asparagine (Q/N)-rich domains have a high propensity to form self-propagating amyloid fibrils. This phenomenon underlies both prion-based inheritance in yeast and aggregation of a number of proteins involved in human neurodegenerative diseases. To examine the prevalence of this phenomenon, complete proteomic sequences of 31 organisms and several incomplete proteomic sequences were examined for Q/N-rich regions. We found that Q/N-rich regions are essentially absent from the thermophilic bacterial and archaeal proteomes. Moreover, the average Q/N content of the proteins in these organisms is markedly lower than in mesophilic bacteria and eukaryotes. Mesophilic bacterial proteomes contain a small number (0-4) of proteins with Q/N-rich regions. Remarkably, Q/N-rich domains are found in a much larger number of eukaryotic proteins (107-472 per proteome) with diverse biochemical functions. Analyses of these regions argue they have been evolutionarily selected perhaps as modular "polar zipper" protein-protein interaction domains. These data also provide a large pool of potential novel prion-forming proteins, two of which have recently been shown to behave as prions in yeast, thus suggesting that aggregation or prion-like regulation of protein function may be a normal regulatory process for many eukaryotic proteins with a wide variety of functions.
Proceedings of the National Academy of Sciences of the United States of America © 2000 National Academy of Sciences