Abstract Increasing evidence suggests that ribosomes actively regulate protein synthesis. However, much of this evidence is indirect, leaving this layer of gene regulation largely unexplored, in part due to methodological limitations. Indeed, evidence is reviewed demonstrating that commonly used methods, such as transcriptomics, are inadequate because the variability in mRNAs coding for ribosomal proteins (RP) does not necessarily correspond to RP variability. Thus protein remodeling of ribosomes should be investigated by methods that allow direct quantification of RPs, ideally of isolated ribosomes. Such methods are reviewed, focusing on mass spectrometry and emphasizing method-specific biases and approaches to control these biases. It is argued that using multiple complementary methods can help reduce the danger of interpreting reproducible systematic biases as evidence for ribosome remodeling.
slavovLabThe monthly video of the lecture series 𝑺𝒕𝒂𝒕𝒊𝒔𝒕𝒊𝒄𝒔 𝒇𝒐𝒓 𝒑𝒓𝒐𝒕𝒆𝒐𝒎𝒊𝒄𝒔 is focused on non-ignorable missing data.
Ignoring non-ignorable missingness leads to survivor bias & other artifacts t.co/v4rlCT2lust.co/HHmH8qVBbw