Primary structure of rat ribosomal protein S2. A ribosomal protein with arginine-glycine tandem repeats and RGGF motifs that are associated with nucleolar localization and binding to ribonucleic acids.

Suzuki, Katsuyuki; Olvera, Joe; Wool, Ira G.

doi:10.1016/s0021-9258(18)54884-5

Cited by 46 publications

(2 citation statements)

References 37 publications

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“…This gene codes the 40S ribosomal protein S2 (RPS2) in rats, a protein responsible for aminoacyl-tRNA binding. This protein is similar to yeast S4 and Escherichia coli S5 ribosomal proteins [ 50 ]. Upregulation of AC136661.1 may permit the fidelity of the translation of mRNA ribosomes in mitochondria which guarantee the supply of energy in MGB neurons [ 51 ].…”

Section: Discussionmentioning

confidence: 99%

Transcriptional-profile changes in the medial geniculate body after noise-induced tinnitus

Liu,

Xue,

Zhang

et al. 2024

Exp. Biol. Med.

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Tinnitus is a disturbing condition defined as the occurrence of acoustic hallucinations with no actual sound. Although the mechanisms underlying tinnitus have been explored extensively, the pathophysiology of the disease is not completely understood. Moreover, genes and potential treatment targets related to auditory hallucinations remain unknown. In this study, we examined transcriptional-profile changes in the medial geniculate body after noise-induced tinnitus in rats by performing RNA sequencing and validated differentially expressed genes via quantitative polymerase chain reaction analysis. The rat model of tinnitus was established by analyzing startle behavior based on gap-pre-pulse inhibition of acoustic startles. We identified 87 differently expressed genes, of which 40 were upregulated and 47 were downregulated. Pathway-enrichment analysis revealed that the differentially enriched genes in the tinnitus group were associated with pathway terms, such as coronavirus disease COVID-19, neuroactive ligand-receptor interaction. Protein–protein-interaction networks were established, and two hub genes (Rpl7a and AC136661.1) were identified among the selected genes. Further studies focusing on targeting and modulating these genes are required for developing potential treatments for noise-induced tinnitus in patients.

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Section: Discussionmentioning

confidence: 99%

Transcriptional-profile changes in the medial geniculate body after noise-induced tinnitus

Liu,

Xue,

Zhang

et al. 2024

Exp. Biol. Med.

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“…L42996) containing sequences encoding only the mature preprotein [23,24] ; CHOB [25] (kindly provided by Dr. R. Rohan) ; argininosuccinate synthetase (AS) and lyase (AL) cDNAs [26,27] (kindly provided by Dr. Marian Jackson). The 0.6 kb EcoR1-BamH1 fragment of CHOB detects a single RNA species in rodents and is considered to be the mRNA for ribosomal protein S2 [28]. This hamster sequence is 95 % identical to the rat cDNA sequence for ribosomal protein S2 (Genbank accession no.…”

Section: Dna Probesmentioning

confidence: 99%

Effects of insulin on the regulation of branched-chain α-keto acid dehydrogenase E1α subunit gene expression

Costeas

Chinsky

1996

Biochemical Journal

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Alterations in dietary intake, especially of protein, may produce changes in the hepatic levels of the branched-chain alpha-keto acid dehydrogenase (BCKAD) complex. The possible role of insulin in the regulation of these observed changes in hepatic capacity for BCKAD expression was therefore examined. Steady-state RNA levels encoding three of the subunits, E1 alpha, E1 beta and E2, increased by 2-4-fold in the livers of mice starved for 3 days, a known hypoinsulinaemic state. In contrast, the levels of E1 beta and E2, but not E1 alpha, RNA were decreased when mice were fed 0% protein diets compared with the levels observed in mice fed standard (23%) or higher protein isocaloric diets. BCKAD subunit protein levels under these conditions changed co-ordinately even though the changes in RNA were not co-ordinate. The effects of hormonal changes that might be associated with these dietary changes were examined, using the rodent hepatoma cell line H4IIEC3. In these cells, the levels of E1 alpha protein and mRNA were significantly depressed in the presence of insulin. In contrast, the levels of E1 beta and E2 RNAs were not decreased by insulin. The half-lives of the E1 alpha and E2 RNAs were determined to be quite long, from 13 to 18 h, with insulin having no dramatic overall effect on the half-lives determined over 24 h. Therefore, it is likely that insulin directly affects the transcription of the E1 alpha gene rather than RNA stability in exerting its negative regulatory effect. This effect is specific to the E1 alpha subunit. The differences in BCKAD subunit RNA levels observed under various nutritional and developmental conditions may therefore be the result of the differential effects of insulin and other hormones on the multiple regulatory mechanisms modulating BCKAD subunit expression.

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Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box.

1992

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Heterogeneous nuclear ribonucleoproteins (hnRNPs) are thought to influence the structure of hnRNA and participate in the processing of hnRNA to mRNA. The hnRNP U protein is an abundant nucleoplasmic phosphoprotein that is the largest of the major hnRNP proteins (120 kDa by SDS‐PAGE). HnRNP U binds pre‐mRNA in vivo and binds both RNA and ssDNA in vitro. Here we describe the cloning and sequencing of a cDNA encoding the hnRNP U protein, the determination of its amino acid sequence and the delineation of a region in this protein that confers RNA binding. The predicted amino acid sequence of hnRNP U contains 806 amino acids (88,939 Daltons), and shows no extensive homology to any known proteins. The N‐terminus is rich in acidic residues and the C‐terminus is glycine‐rich. In addition, a glutamine‐rich stretch, a putative NTP binding site and a putative nuclear localization signal are present. It could not be defined from the sequence what segment of the protein confers its RNA binding activity. We identified an RNA binding activity within the C‐terminal glycine‐rich 112 amino acids. This region, designated U protein glycine‐rich RNA binding region (U‐gly), can by itself bind RNA. Furthermore, fusion of U‐gly to a heterologous bacterial protein (maltose binding protein) converts this fusion protein into an RNA binding protein. A 26 amino acid peptide within U‐gly is necessary for the RNA binding activity of the U protein. Interestingly, this peptide contains a cluster of RGG repeats with characteristic spacing and this motif is found also in several other RNA binding proteins. We have termed this region the RGG box and propose that it is an RNA binding motif and a predictor of RNA binding activity.

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Primary structure of rat ribosomal protein S2. A ribosomal protein with arginine-glycine tandem repeats and RGGF motifs that are associated with nucleolar localization and binding to ribonucleic acids.

Cited by 46 publications

References 37 publications

Transcriptional-profile changes in the medial geniculate body after noise-induced tinnitus

Transcriptional-profile changes in the medial geniculate body after noise-induced tinnitus

Effects of insulin on the regulation of branched-chain α-keto acid dehydrogenase E1α subunit gene expression

Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box.

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