AI Article Synopsis
- Recognition of polyubiquitinated substrates by the 26S proteasome is crucial for degrading specific cellular proteins, with the Rpn10 subunit playing a key role in this process.
- Researchers explored the diversity of Rpn10, noting that its mRNA is created from a single gene via alternative splicing, which is regulated during development.
- The study shows that this alternative splicing mechanism is not unique to mice, as evidence of distinct Rpn10 forms generated by splicing has been found in lower vertebrates, indicating an evolutionary conservation of this process.
Article Abstract
Recognition of polyubiquitinated substrates by the 26S proteasome is a key step in the selective degradation of various cellular proteins. The Rpn10 subunit of the 26S proteasome can bind polyubiquitin conjugates in vitro. We have previously reported the unique diversity of Rpn10, which differs from other multiple proteasome subunits, and that the mouse Rpn10 mRNA family is generated from a single gene by developmentally regulated alternative splicing. To determine whether such alternative splicing mechanisms occur in other species, we searched for Rpn10 isoforms in databases and in our original PCR products. Here we report the genomic organization of the Rpn10 gene in lower vertebrates and provide evidence for the competent generation of distinct forms of Rpn10 by alternative splicing through evolution.
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| http://dx.doi.org/10.1515/BC.2002.139 | DOI Listing |
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