Increased ribosomal affinity for mRNA causes resistance to edeine in a mutant of <i>Saccharomyces cerevisiae</i>

Herrera, Flor; Moreno, Nancy; Martinez, José A.

doi:10.1111/j.1432-1033.1984.tb08559.x

Cited by 8 publications

(3 citation statements)

References 32 publications

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“…The only mutant resistant to edeine that has been functionally characterized is a mutant of Saccharomyces cerevisiae . This mutant overcomes edeine inhibition by an increased affinity for mRNA (Herrera et al ., 1984). In eukaryotes, where the initial docking of the mRNA is independent of base complementarity between the mRNA and the 18S rRNA, an increased affinity of the small subunit for mRNA could indeed promote edeine resistance.…”

Section: Discussionmentioning

confidence: 99%

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

et al. 2001

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The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X-ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A-site inhibitor tetracycline, the universal initiation inhibitor edeine and the C-terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A-site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P-site tRNA. The location of the C-terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti-association activity of IF3 is due to its in¯uence on the conformational dynamics of the small ribosomal subunit.

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Section: Discussionmentioning

confidence: 99%

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

et al. 2001

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“…Isolation of ribosomes -The ribosomes were isolated according to Herrera et al (1984). Some aliquots were treated with high salt and were labeled as high salt ribosomes (HSR).…”

Section: Methodsmentioning

confidence: 99%

An in vitro system from Plasmodium falciparum active in endogenous mRNA translation

Ferreras

Triana

Correia

et al. 2000

Mem. Inst. Oswaldo Cruz

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“…All of the preincubations, incubations and gradients were pcrformcd with 3 mM Mg2+ except in B where 5 mM was used Herrera et al [16], with 50-70 pg HSRW or with 0.1 -0.5 pg purified A F in a final volume of 200 pl. The incubations were layered on and centrifuged through 10 -32% linear gradients of sucrose in buffer A (buffer B without glycerol) as described by Gasior et al [17].…”

Section: Assuyfor Ribosomal Subunits Association Factor (Afj Activitymentioning

confidence: 99%

Association of ribosomal subunits

Herrera

Correia

Triana

et al. 1991

European Journal of Biochemistry

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A yeast ribosomal subunit association factor (AF) has been purified from a high-salt ribosomal wash. The purified enzyme is a thermostable protein that associates ribosomal subunits at low Mg2 + concentration without requiring energy. It appears to be an aggregate of trimers or dimers (molecular mass 125 or 79 kDa) which on sodium dodecyl sulfate gels shows the presence of a major protein band whose estimated molecular mass is 43 kDa. Evidence also indicates the existence of a 50-kDa polypeptide which seems to be unstable since with freezing and thawing it gives rise to the 43-kDa polypeptide. It was shown that the labelled factor interacts with 80s ribosomes and with 40s ribosomal subunits. The purified polypeptide reacts with antibodies directed against EF-la, this last protein recognizing the antibodies raised against AF. Likewise, both EF-la and AF associate ribosomal subunits in the same way. When EF-1 is heated, it not only maintains its association activity, but also behaves like a 43-kDa polypeptide in an SDS electrophoresis run. These observations strongly suggest that AF originates from EF-la, which implies that the well-known elongation factor may also play a role in the initiation step of protein synthesis.In the ribosomal cycle, when the ribosomal subunits are released at chain termination they may bind factors which prevent their reassociation and channel them into another cycle of synthesis, or they may recombine and enter the pool of monomers. In prokaryotic and eukaryotic cells, the monomer ribosomes accumulate at the expense of polysome degradation that takes place when protein synthesis diminishes under a variety of metabolically adverse conditions [l]. These single ribosomes can revert to polysomes when the rate of overall protein synthesis increases and in this way function as a reserve of potential subunits. This fluctuation in the rate of protein synthesis and the corresponding monomer level, which are not necessarily related to growth, may occur normally in eukaryotic cells. Such regulation may reflect variations in the activity of some factor or group of factors that participates either in the ribosomal subunit association or in the dissociation step. The interdependence between these two kinds of factors will determine whether subunits, released at peptide chain termination, will immediately reassociate with mRNA to initiate another round of synthesis or will couple and enter the pool of inactive monomers.Earlier studies have established that ribosomes are in dynamic equilibrium with their subunits [2-51. Vast amounts of information accumulated in the last two decades point to the existence of initiation factors that prevents the association of ribosomal subunits into single ribosomes but does not actively promote their dissociation. Dissociation of single ribosomes can take place spontaneously at low magnesium concentration, thereby generating subunits which are unable to revert to monosomes because binding of eIF-3 and eIF-4C to 40s subunits and binding of eIF-6 to 60s subunits block ...

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Increased ribosomal affinity for mRNA causes resistance to edeine in a mutant of Saccharomyces cerevisiae

Cited by 8 publications

References 32 publications

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

An in vitro system from Plasmodium falciparum active in endogenous mRNA translation

Association of ribosomal subunits

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