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Researchers discover critical detail of cellular defense against genetic mistakes
Date:4/17/2008

steady-state rounds then direct the mass production of normal proteins based on NMD-approved mRNAs. Over time, the Maquat lab, along with other labs, has identified a number of protein complexes that form during the intricate process by which cells analyze each mRNA for flaws.

In the past, her team showed, for instance, which proteins bind to each end of mRNA during the pioneer and subsequent steady-state rounds of translation, and how the pioneer round, cap-binding protein promotes the recognition and decay of flawed mRNAs. The team also demonstrated how other complexes that identify flawed mRNAs form near exon-exon junctions, the places where each must read section of the mature mRNA template is joined to the next by RNA splicing.

Past work by Maquats team further revealed that much of the NMD quality review depends on the physical spacing of proteins bound to the mRNA chain. If a stop reading signal occurs too far ahead of the final exon in the chain, as marked by an exon-exon junction complex (EJC), the cell concludes that the stop codon has mistakenly fallen in the middle of a set of instructions. These mRNAs are degraded. They also found that the EJC contains human up-frameshift (UPF) proteins that play a role in NMD.

In their latest search for detail, Maquat and colleagues determined that the delivery of a given faulty mRNA to the degradation machinery requires first the active shutdown (translational repression) of protein building based on that mRNA. In the studys key finding, experiments revealed that repression of protein synthesis during NMD is controlled the attachment of phosphate groups to human UPF1, researchers said. Human cells have evolved such that phosphorylation, the attachment of phosphate groups to proteins, is used in many scenarios like a switch to turn processes on or off.

Based on their findings, Maquat and colleagues propose the following new model for NMD: When a nonsense stop codon is detected,
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Contact: Greg Williams
Greg_Williams@urmc.rochester.edu
University of Rochester Medical Center
Source:Eurekalert

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