Depurination of A4256 in 28 S rRNA by the Ribosome-inactivating Proteins from Barley and Ricin Results in Different Ribosome Conformations

Holmberg, Lovisa; Nygård, Odd

doi:10.1006/jmbi.1996.0303

Cited by 15 publications

(7 citation statements)

References 55 publications

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“…These findings suggest that the regional structure of sarcin domain may be changed when the 3) side nucleotides of the domain are contacted by a complementary oligo DNA. This seems reasonable since the conformational change of the sarcin domain has been suggested to occur when ribosomes are engaged in the translocation with translational factors [8,15,19,23,24,39] or are contacted by oligo DNA [19,24]. However, results of this study provide direct evidence of dynamic change of the sarcin domain.…”

Section: Discussioncontrasting

confidence: 53%

Probing Surface Structure of Sarcin Domain on Ribosomes of <i>Escherichia coli</i> by Complementary Oligo DNAs and Ribosome-Inactivating Protein

Cheung¹,

Lin²

1999

J Biomed Sci

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The regional structure of the sarcin domain of 23S rRNA of Escherichia coli ribosomes was determined by a combinatory approach of oligo DNA probes and the action of α-sarcin. The sarcin domain is protected by a reactive complementary oligo DNA probe against the hydrolytic action of α-sarcin. This protective effect is dependent upon the length and the complementary sequence of oligo DNA probes that react to ribosomes. Under UV irradiation and using of the primer extension, nucleotides that contacted by reactive oligo DNA probes were determined. Nucleotides at the 3′ side of the domain (positions from G2659 to C2676) were targeted by oligo DNA probes that have their sequences to complement the domain, indicating that the 3′ side region was exposed on the surface of ribosomes, whereas nucleotides at the 5′ side of stem and extented to two bases at the loop (positions from C2646 to A2654) were not accessible to any oligo DNA probes, implying that the region could be buried in ribosomes. This study also provided evidence that the conformation of the sarcin domain is subjected to alteration if the exposed 3′ side of domain is targeted by the reactive DNA probe. The importance of the topological arrangement of the sarcin domain that engages in the translocation event during translation is discussed.

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Section: Discussioncontrasting

confidence: 53%

Probing Surface Structure of Sarcin Domain on Ribosomes of <i>Escherichia coli</i> by Complementary Oligo DNAs and Ribosome-Inactivating Protein

Cheung¹,

Lin²

1999

J Biomed Sci

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“…It promotes selective depurination of one base in the larger rRNA molecule (22). This modification destroys the dynamic properties of the ribosome, freezing the particle in a single conformation that has been identified with the POST ribosome (23). Fig.…”

Section: Resultsmentioning

confidence: 99%

Sordarin Inhibits Fungal Protein Synthesis by Blocking Translocation Differently to Fusidic Acid

Domínguez¹,

Gómez-Lorenzo²,

Martin³

1999

Journal of Biological Chemistry

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Sordarin derivatives are selective inhibitors of fungal protein synthesis, which specifically impair elongation factor 2 (EF-2) function. We have studied the effect of sordarin on the ribosome-dependent GTPase activity of EF-2 from Candida albicans in the absence of any other component of the translation system. The effect of sordarin turned out to be dependent both on the ratio of ribosomes to EF-2 and on the nature of the ribosomes. When the amount of EF-2 exceeded that of ribosomes sordarin inhibited the GTPase activity following an inverted bell-shaped dose-response curve, whereas when EF-2 and ribosomes were in equimolar concentrations sordarin yielded a typical sigmoidal dose-dependent inhibition. However, when ricin-treated ribosomes were used, sordarin stimulated the hydrolysis of GTP. These results were compared with those obtained with fusidic acid, showing that both drugs act in a different manner. All these data are consistent with sordarin blocking the elongation cycle at the initial steps of translocation, prior to GTP hydrolysis. In agreement with this conclusion, sordarin prevented the formation of peptidyl-[ 3 H]puromycin on polysomes from Candida albicans.

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“…In recent years, their cytotoxicity has been exploited for the development of immunotoxins for tumor therapy [3][4][5] as well as for applications as abortifacients and anti-human immunodeficiency virus (HIV) agents [2]. RIPs target a universally conserved sequence of the ribosome alpha-sarcin loop, which is also involved in the binding of elongation factors to the ribosome [6]. Despite the large amount of structural information on the ribosome accumulated recently [7][8][9], no detailed information is still known on the mode of interaction of RIPs with ribosomes.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L4, a Ribosome Inactivating Protein from Phytolacca dioica L. leaves

Ruggiero¹,

Maro²,

Pisante³

et al. 2007

PPL

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PD-L4, a type 1 ribosome inactivating protein from Phytolacca dioica leaves, has been successfully crystallized using vapour diffusion methods and PEG 4000 as a precipitant agent. In addition, crystals of a PD-L4 mutant, which has been recently observed to have a lower polynucleotide-adenosine glycosidase activity on DNA, rRNA and poly (A) substrates, have been obtained. To gather information on PD-L4 reaction mechanism both forms have been co-crystallized with adenine, the major product of their catalytic reaction. Diffraction patterns extend to atomic resolution and crystals belong to the orthorhombic P2(1)2(1)2(1) space group, with one molecule in the asymmetric unit. Structure determination has been achieved using molecular replacement; preliminary electron density maps have clearly given evidence of adenine binding.

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Depurination of A4256 in 28 S rRNA by the Ribosome-inactivating Proteins from Barley and Ricin Results in Different Ribosome Conformations

Cited by 15 publications

References 55 publications

Probing Surface Structure of Sarcin Domain on Ribosomes of <i>Escherichia coli</i> by Complementary Oligo DNAs and Ribosome-Inactivating Protein

Probing Surface Structure of Sarcin Domain on Ribosomes of <i>Escherichia coli</i> by Complementary Oligo DNAs and Ribosome-Inactivating Protein

Sordarin Inhibits Fungal Protein Synthesis by Blocking Translocation Differently to Fusidic Acid

Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L4, a Ribosome Inactivating Protein from Phytolacca dioica L. leaves

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