2023
DOI: 10.3390/biom13050853
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Ribosomal Protein uS5 and Friends: Protein–Protein Interactions Involved in Ribosome Assembly and Beyond

Abstract: Ribosomal proteins are fundamental components of the ribosomes in all living cells. The ribosomal protein uS5 (Rps2) is a stable component of the small ribosomal subunit within all three domains of life. In addition to its interactions with proximal ribosomal proteins and rRNA inside the ribosome, uS5 has a surprisingly complex network of evolutionarily conserved non-ribosome-associated proteins. In this review, we focus on a set of four conserved uS5-associated proteins: the protein arginine methyltransferase… Show more

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Cited by 5 publications
(3 citation statements)
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References 100 publications
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“…As we all know, ribosomal proteins play an important part in ribosome assembly. They combine with four ribosomal RNAs (rRNAs) to form the ribosomal subunits, which have an important function cellular protein translation ( Landry-Voyer et al, 2023 ). Consistent with our findings, reference genes involving ribosomal protein genes have been selected frequently for expression analysis in various insects during the last 10 years ( Zhang et al, 2022 ; Shen et al, 2022 ).…”
Section: Discussionmentioning
confidence: 99%
“…As we all know, ribosomal proteins play an important part in ribosome assembly. They combine with four ribosomal RNAs (rRNAs) to form the ribosomal subunits, which have an important function cellular protein translation ( Landry-Voyer et al, 2023 ). Consistent with our findings, reference genes involving ribosomal protein genes have been selected frequently for expression analysis in various insects during the last 10 years ( Zhang et al, 2022 ; Shen et al, 2022 ).…”
Section: Discussionmentioning
confidence: 99%
“…Among the proteins found in our analysis, there were many ribosomal proteins, which are a variety of proteins that compose the ribosome and participate in the folding of rRNA molecules into a structure that is required for the interaction of mRNA codons and tRNA anticodons ( Landry-Voyer et al., 2023 ). We excluded this class of proteins to avoid bias toward translation.…”
Section: Discussionmentioning
confidence: 99%
“…Intriguingly, Rps2's unstructured N-terminal region seems to be a hub for the binding of multiple interaction partners (elaborated in detail in a review article by the Bachand group within this Special Issue [39]). Besides the binding partners investigated in this study (Tsr4 and importins), the N-terminal part of Rps2 also likely interacts (at least transiently) with Hmt1, as this enzyme methylates an arginine in the N-terminal region of Rps2 [40,41].…”
Section: Discussionmentioning
confidence: 99%