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Scripps Research scientists solve long-standing mystery of protein 'quality control' mechanism
Date:9/12/2010

yeast S. cerevisiae as a model organism. Yeast is complex enough to share many cellular features with other eukaryotes such as mice and humans, yet relatively simple to work with in the lab. Most importantly, since it possesses a short lifecycle, yeast experiments can yield results more quickly.

When the results were in, they showed that cells without Listerin (called Ltn1 in yeast) failed to get rid of non-stop proteins and died when those proteins were produced. Ltn1 was the long-sought missing link for non-stop protein degradationeven though it looked nothing like tmRNA/ssrA.

In addition to revealing Ltn1's function, in the study the scientists went on to describe the mechanism by which it worked. Joazeiro and Bengtson found that Ltn1 binds to ribosomes and tags nascent non-stop proteins with ubiquitin moleculesa common signal for protein destruction in cells of eukaryotic organisms.

"The [bacterial and eukaryotic] mechanisms are very different, but the concepts are remarkably similarthat's the beauty of it," said Joazeiro. "It also turns out that in the same way that the tmRNA molecule is conserved in all bacteria, Listerin is conserved in all eukaryotes, which once again highlights its importance. It appears that between tmRNA and Listerin we have coverage throughout most living organisms of the surveillance of these defective proteins."

While the study solves a fundamental biological mystery, many questions remain. To what extent is this process similar in mice or humans? Would a defect in Listerin's role in protein quality control account for the neurodegeneration in the mutant mice? Are there human neurodegenerative diseases caused by Listerin mutation? The Joazeiro lab continues to investigate.


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Contact: Mika Ono
mikaono@scripps.edu
858-784-2052
Scripps Research Institute
Source:Eurekalert

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