Mutation at the Site of Hydroxylation in the Ribosomal Protein uL15 (RPL27a) Causes Specific Changes in the Repertoire of mRNAs Translated in Mammalian Cells

Zolotenkova, Elizaveta A.; Gopanenko, Alexander V.; Tupikin, Alexey E.; Kabilov, Мarsel R.; Malygin, Alexey A.

doi:10.3390/ijms24076173

Cited by 3 publications

(2 citation statements)

References 33 publications

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“…In the cells producing the mutant protein derived from the abilit of the specific hydroxylation, its content in polysomes was less than that of the wild typ RP uL15. On the other hand, the mutation did not affect incorporation of the RP uL15 int the 60S subunits or into the 80S ribosomes; however, it caused specific changes to the rep ertoire of translated mRNAs [81]. These findings indicate the significance of the hydrox ylation of RP uL15 at H39 for translation elongation in living human cells.…”

Section: Hydroxylated H39 Of the Rp Ul15 (Rpl27a) At The Region Close...mentioning

confidence: 83%

Two “Edges” in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes

Ochkasova

Arbuzov

Malygin

et al. 2023

IJMS

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Ribosomal proteins (RPs), the constituents of the ribosome, belong to the most abundant proteins in the cell. A highly coordinated network of interactions implicating RPs and ribosomal RNAs (rRNAs) forms the functionally competent structure of the ribosome, enabling it to perform translation, the synthesis of polypeptide chain on the messenger RNA (mRNA) template. Several RPs contact ribosomal ligands, namely, those with transfer RNAs (tRNAs), mRNA or translation factors in the course of translation, and the contribution of a number of these particular contacts to the translation process has recently been established. Many ribosomal proteins also have various extra-ribosomal functions unrelated to translation. The least-understood and -discussed functions of RPs are those related to their participation in the intercellular communication via extracellular vesicles including exosomes, etc., which often carry RPs as passengers. Recently reported data show that such a kind of communication can reprogram a receptor cell and change its phenotype, which is associated with cancer progression and metastasis. Here, we review the state-of-art ideas on the implications of specific amino acid residues of RPs in the particular stages of the translation process in higher eukaryotes and currently available data on the transport of RPs by extracellular vesicles and its biological effects.

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Section: Hydroxylated H39 Of the Rp Ul15 (Rpl27a) At The Region Close...mentioning

confidence: 83%

Two “Edges” in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes

Ochkasova

Arbuzov

Malygin

et al. 2023

IJMS

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“…Ribosomes are the intracellular machinery required for translating specific mRNAs [1]. This machinery synthesizes new proteins based on the sequence of mRNA codons, and precise correction is determined by correct folding by the ribosome [2]. Ribosomal components include ribosomal proteins (RPs) and ribosomal RNA (rRNA).…”

Section: Introductionmentioning

confidence: 99%

The Effects of Deregulated Ribosomal Biogenesis in Cancer

Lu,

Wang,

Jiao

2023

Biomolecules

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Ribosomes are macromolecular ribonucleoprotein complexes assembled from RNA and proteins. Functional ribosomes arise from the nucleolus, require ribosomal RNA processing and the coordinated assembly of ribosomal proteins (RPs), and are frequently hyperactivated to support the requirement for protein synthesis during the self-biosynthetic and metabolic activities of cancer cells. Studies have provided relevant information on targeted anticancer molecules involved in ribosome biogenesis (RiBi), as increased RiBi is characteristic of many types of cancer. The association between unlimited cell proliferation and alterations in specific steps of RiBi has been highlighted as a possible critical driver of tumorigenesis and metastasis. Thus, alterations in numerous regulators and actors involved in RiBi, particularly in cancer, significantly affect the rate and quality of protein synthesis and, ultimately, the transcriptome to generate the associated proteome. Alterations in RiBi in cancer cells activate nucleolar stress response-related pathways that play important roles in cancer-targeted interventions and immunotherapies. In this review, we focus on the association between alterations in RiBi and cancer. Emphasis is placed on RiBi deregulation and its secondary consequences, including changes in protein synthesis, loss of RPs, adaptive transcription and translation, nucleolar stress regulation, metabolic changes, and the impaired ribosome biogenesis checkpoint.

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Visualizing the modification landscape of the human 60S ribosomal subunit at close to atomic resolution

Wiechert,

Unbehaun,

Sprink

et al. 2024

Nucleic Acids Research

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Chemical modifications of ribosomal RNAs (rRNAs) and proteins expand their topological repertoire, and together with the plethora of bound ligands, fine-tune ribosomal function. Detailed knowledge of this natural composition provides important insights into ribosome genesis and function and clarifies some aspects of ribosomopathies. The discovery of new structural properties and functional aspects of ribosomes has gone hand in hand with cryo-electron microscopy (cryo-EM) and its technological development. In line with the ability to visualize atomic details – a prerequisite for identifying chemical modifications and ligands in cryo-EM maps – in this work we present the structure of the 60S ribosomal subunit from HeLa cells at the very high global resolution of 1.78 Å. We identified 113 rRNA modifications and four protein modifications including uL2-Hisβ-ox216, which stabilizes the local structure near the peptidyl transferase centre via an extended hydrogen-bonding network. We can differentiate metal ions Mg2+ and K+, polyamines spermine, spermidine and putrescine and identify thousands of water molecules binding to the 60S subunit. Approaching atomic resolution cryo-EM has become a powerful tool to examine fine details of macromolecular structures that will expand our knowledge about translation and other biological processes in the future and assess the variability of the chemical space due to differences between species/tissues or varying physicochemical environment.

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Mutation at the Site of Hydroxylation in the Ribosomal Protein uL15 (RPL27a) Causes Specific Changes in the Repertoire of mRNAs Translated in Mammalian Cells

Cited by 3 publications

References 33 publications

Two “Edges” in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes

Two “Edges” in Our Knowledge on the Functions of Ribosomal Proteins: The Revealed Contributions of Their Regions to Translation Mechanisms and the Issues of Their Extracellular Transport by Exosomes

The Effects of Deregulated Ribosomal Biogenesis in Cancer

Visualizing the modification landscape of the human 60S ribosomal subunit at close to atomic resolution

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