Analyzing Ribosome Remodeling in Health and Disease

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, suc...

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Published inProteomics (Weinheim) Vol. 20; no. 17-18; pp. e2000039 - n/a
Main Authors Petelski, Aleksandra A., Slavov, Nikolai
Format Journal Article
LanguageEnglish
Published Weinheim Wiley Subscription Services, Inc 01.09.2020
Subjects
complementary mass spectrometry methods
Gene regulation
Mass spectrometry
Mass spectroscopy
post‐transcriptional regulation
Protein biosynthesis
Protein synthesis
Proteins
Reviews
Ribosomal proteins
ribosome specialization
Ribosomes
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Summary: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.
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ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.202000039