2020/07/31 by Aleksandra A. Petelski, Nikolai Slavov · 14 citations
Biochemistry, Genetics and Molecular Biology · Immunology and Microbiology · #Gene #Messenger RNA #Proteomics #RNA and protein synthesis mechanisms #RNA modifications and cancer #Ribosomal RNA #Ribosomal protein #Ribosome #Ribosome profiling #Toxin Mechanisms and Immunotoxins #Translation (biology) #q-bio.BM #q-bio.MN #q-bio.QM #q-bio.SC
paper · pdf · doi:10.1002/pmic.202000039
published in PROTEOMICS 20(17-18), e2000039 (Wiley)
openalex created_date 2020/07/16 · arxiv created 2020/08/02 · openalex publication_date 2020/08/21 · arxiv updated 2020/09/01 · openalex updated_date 2026/08/05
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.