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Ribosomal proteins: functions beyond the ribosome [PDF]
Journal of Molecular Cell Biology, 2015 Although ribosomal proteins are known for playing an essential role in ribosome assembly and protein translation, their ribosome-independent functions have also been greatly appreciated. Over the past decade, more than a dozen of ribosomal proteins have been found to activate the tumor suppressor p53 pathway in response to ribosomal stress. In addition,
Xiang, Zhou +4 more
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eLife, 2022 Rapid and accurate mRNA translation requires efficient codon-dependent delivery of the correct aminoacyl-tRNA (aa-tRNA) to the ribosomal A site. In mammals, this fidelity-determining reaction is facilitated by the GTPase elongation factor-1 alpha (eEF1A),
Manuel F Juette +9 more
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Hepatitis C virus 3'UTR regulates viral translation through direct interactions with the host translation machinery. [PDF]
, 2013 The 3' untranslated region (3'UTR) of hepatitis C virus (HCV) messenger RNA stimulates viral translation by an undetermined mechanism. We identified a high affinity interaction, conserved among different HCV genotypes, between the HCV 3'UTR and the host ...
Bai, Yun +2 more
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Ribosome-omics of the human ribosome [PDF]
RNA, 2014 The torrent of RNA-seq data becoming available not only furnishes an overview of the entire transcriptome but also provides tools to focus on specific areas of interest. Our focus on the synthesis of ribosomes asked whether the abundance of mRNAs encoding ribosomal proteins (RPs) matched the equimolar need for the RPs in the assembly of ribosomes.
Gupta, Varun, Warner, Jonathan R.
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Active role of elongation factor G in maintaining the mRNA reading frame during translation. [PDF]
, 2019 During translation, the ribosome moves along the mRNA one codon at a time with the help of elongation factor G (EF-G). Spontaneous changes in the translational reading frame are extremely rare, yet how the precise triplet-wise step is maintained is not ...
Belardinelli, R. +5 more
core +2 more sources
eLife, 2017 Ribosome stalling on mRNAs can decrease protein expression. To decipher ribosome kinetics at stall sites, we induced ribosome stalling at specific codons by starving the bacterium Escherichia coli for the cognate amino acid. We measured protein synthesis
Michael A Ferrin, Arvind R Subramaniam
doaj +1 more source
Cotranslational folding of proteins on the ribosome.
, 2020 Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways ...
Liutkute, M., Rodnina, M., Samatova, E.
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Ribosomal Proteins in Ribosome Assembly
BiomoleculesRibosomes are the cellular machinery responsible for translating mRNA into proteins, a process fundamental to all domains of life from bacteria to eukaryotes [...]
Brigitte Pertschy, Ingrid Zierler
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Plants, 2020 Bacterial ribosome hibernation factors sequester ribosomes in an inactive state during the stationary phase and in response to stress. The cyanobacterial ribosome hibernation factor LrtA has been suggested to inactivate ribosomes in the dark and to be ...
Kevin Swift +4 more
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Microtubule-dependent ribosome localization in C. elegans neurons. [PDF]
, 2017 Subcellular localization of ribosomes defines the location and capacity for protein synthesis. Methods for in vivo visualizing ribosomes in multicellular organisms are desirable in mechanistic investigations of the cell biology of ribosome dynamics. Here,
Ellisman, Mark H +3 more
core +1 more source