Key result
Ribosome profiling reveals how translating ribosomes tune maturation and avoid degradation during necessary pausing.
Why the study?
The mechanisms by which ribosome pausing regulates co-translational protein maturation and avoids degradation during necessary pauses remain to be fully understood.
Key points are not available for this paper at this time.
Design
Review summarizing recent studies using ribosome profiling
Extends molecular frameworks for co-translational events; leaves open validation in cardiovascular models or trials.
In recent years translation elongation has emerged as an important contributor to the regulation of gene expression. There are multiple quality control checkpoints along the way of producing mature proteins and targeting them to the right cellular compartment, or associating them correctly with their partners. Ribosomes pause to allow co-translational protein folding, protein targeting or protein interactions, and the pausing is dictated by a combination of the mRNA sequence and structure, the tRNA availability and the nascent peptide. However, ribosome pausing can also lead to ribosome collisions and co-translational degradation of both mRNA and nascent chain. Understanding how the translating ribosome tunes the different maturation steps that nascent proteins must undergo, what the timing of these maturation events is, and how degradation can be avoided when pausing is needed, is now possible by the emergence of methods to follow ribosome dynamics in vivo. This review summarizes some of the recent studies that have advanced our knowledge about co-translational events using the power of ribosome profiling, and some of the questions that have emerged from these studies.
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Collart et al. (2019) reported a review. This review summarizes recent studies using ribosome profiling to understand how translating ribosomes tune maturation steps, timing of events, and avoidance of degradation during necessary pausing.
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