The site of reaction on ribosomal protein L27 with an affinity label derivative of tRNA<sup>met</sup><sub>f</sub>

Collatz, E.; Küchler, E.; Stöffler, Georg; Czernilofsky, P.

doi:10.1016/0014-5793(76)80112-3

Cited by 13 publications

(6 citation statements)

References 8 publications

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“…In eukaryotes, ribosomes have also been detected in mitochondria in addition to the cytoplasm. Interestingly, mammalian mitochondria ribosomes are more similar to prokaryotes 70S ribosomes (Collatz et al, 1976 ). According to the “endosymbiotic theory,” mitochondria are derived from bacteria, that is, after bacteria are swallowed by eukaryotes, in the long-term symbiosis process, they form mitochondria through evolution (Martin et al, 2015 ).…”

Section: Mechanism Of Aminoglycoside Ototoxicitymentioning

confidence: 99%

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

Wan

et al. 2021

Front. Cell. Neurosci.

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Aminoglycosides, a class of clinically important drugs, are widely used worldwide against gram-negative bacterial infections. However, there is growing evidence that aminoglycosides can cause hearing loss or balance problems. In this article, we mainly introduce the main mechanism of ototoxicity induced by aminoglycosides. Genetic analysis showed that the susceptibility of aminoglycosides was attributable to mutations in mtDNA, especially A1555G and C1494T mutations in 12S rRNA. In addition, the overexpression of NMDA receptors and the formation of free radicals also play an important role. Understanding the mechanism of ototoxicity induced by aminoglycosides is helpful to develop new therapeutic methods to protect hearing. In this article, the prevention methods of ototoxicity induced by aminoglycosides were introduced from the upstream and downstream aspects.

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Section: Mechanism Of Aminoglycoside Ototoxicitymentioning

confidence: 99%

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

Wan

et al. 2021

Front. Cell. Neurosci.

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“…4 also demonstrate that S6 is the ribosomal protein phosphorylated by ViPK in the presence of spermine. As the relative molecular mass of purified ribosomal protein S6 is 31000 (Collatz et al, 1976), S6 most likely corresponds to the 31 kDa band of Figs. 1-3.…”

Section: Identification Of Ribosomal Proteins Phosphorylated Bymentioning

confidence: 98%

The phosphorylation of ribosomal protein S6 by protein kinases from cells infected with pseudorabies virus

Katan¹,

McGarvey²,

Stevely³

et al. 1986

Biochemical Journal

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We examined the ability of protein kinase activities from BHK (baby-hamster kidney) cells infected with pseudorabies virus to catalyse the phosphorylation of ribosomal protein S6 in vitro. When the cytosol from infected cells was fractionated on DEAE-cellulose, 40S ribosomal protein kinase activity was found associated with the two isoforms of the cyclic AMP-dependent protein kinase, protein kinase C and a protein kinase (ViPK, virus-induced protein kinase) only detected in infected cells. The phosphorylation of ribosomal protein by ViPK was of particular interest because the appearance of the protein kinase and the increase in the phosphorylation of protein S6 in infected cells shared a similar time course. At moderate concentrations of KCl the major ribosomal substrate for ViPK was ribosomal protein S7, a protein not found to be phosphorylated in vivo. However, at 600 mM-KCl, or in the presence of 5-10 mM-spermine at 60-150 mM-KCl, the phosphorylation of ribosomal protein S7 was suppressed and ribosomal protein S6 became the major substrate. The maximum stoichiometry of phosphorylation obtained under the latter conditions was 1-2 mol of phosphate/mol of S6, and only mono- and di-phosphorylated forms of S6 were detected on two-dimensional gel electrophoresis. As the infection of BHK cells by pseudorabies virus results in the appearance of phosphorylated species of S6 containing up to 5 mol of phosphate/mol of S6 protein, it appears unlikely that ViPK alone can be responsible for the multiple phosphorylation seen in vivo. Nevertheless, tryptic phosphopeptide analysis did indicate that in vitro ViPK catalysed the phosphorylation of at least one of the sites on ribosomal protein S6 phosphorylated in vivo, so that a contributory role for the enzyme in the phosphorylation in vivo cannot be excluded.

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“…For instance, mitochondria use fMet-tRNA as an initiator of protein synthesis. Mammalian mitochondrial ribosomes have small 28S and large 39S subunits, forming a 55S protein complex, which is active in mitochondria and functions to translate mitochondrial mRNAs encoded in mtDNA ( Collatz et al., 1976 ). Even though mitochondria ribosomes are similar to bacterial ribosomes, normal cells show low toxicity to regular dosages of AmAn.…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial DNA mutations associated with aminoglycoside induced ototoxicity

2017

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Aminoglycosides (AmAn) are widely used for their great efficiency against gram-negative bacterial infections. However, they can also induce ototoxic hearing loss, which has affected millions of people around the world. As previously reported, individuals bearing mitochondrial DNA mutations in the 12S rRNA gene, such as m.1555A>G and m.1494C>T, are more prone to AmAn-induced ototoxicity. These mutations cause human mitochondrial ribosomes to more closely resemble bacterial ribosomes and enable a stronger aminoglycoside interaction. Consequently, exposure to AmAn can induce or worsen hearing loss in these individuals. Furthermore, a wide range of severity and penetrance of hearing loss was observed among families carrying these mutations. Studies have revealed that these mitochondria mutations are the primary molecular mechanism of genetic susceptibility to AmAn ototoxicity, though nuclear modifier genes and mitochondrial haplotypes are known to modulate the phenotypic manifestation.

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The site of reaction on ribosomal protein L27 with an affinity label derivative of tRNA^met_f

Cited by 13 publications

References 8 publications

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

The phosphorylation of ribosomal protein S6 by protein kinases from cells infected with pseudorabies virus

Mitochondrial DNA mutations associated with aminoglycoside induced ototoxicity

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The site of reaction on ribosomal protein L27 with an affinity label derivative of tRNAmetf

Cited by 13 publications

References 8 publications

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

Mechanism and Prevention of Ototoxicity Induced by Aminoglycosides

The phosphorylation of ribosomal protein S6 by protein kinases from cells infected with pseudorabies virus

Mitochondrial DNA mutations associated with aminoglycoside induced ototoxicity

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The site of reaction on ribosomal protein L27 with an affinity label derivative of tRNA^met_f