5′‐Secondary structure formation, in constrast to a short string of non‐preferred codons, inhibits the translation of the pyruvate kinase mRNA in yeast

Bettany, A. J. E.; Moore, Paul A.; Cafferkey, Robert; Bell, L. D.; Goodey, A. R.; Carter, Bruce L. A.; Brown, Alistair J. P.

doi:10.1002/yea.320050308

Cited by 45 publications

(29 citation statements)

References 39 publications

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“…Furthermore, the transcription factors encoded by value on lactate. Each assay ABFJ, GCRI, and RAP) are known to influence the expresassays on three independent sion of several glycolytic genes (3,7,13,15,61 (12,60,65).…”

Section: Resultsmentioning

confidence: 99%

“…The RNA was then transferred to Hybond-N membranes (64), UV fixed, and probed with either radiolabeled DNA fragments or oligonucleotides ( Table 1). The adaptions made to previously published hybridization and washing conditions (7,52) for each of the DNA or oligonucleotide probes are summarized in Table 1. Hybridizations were always performed under conditions of probe excess (56).…”

Section: Methodsmentioning

confidence: 99%

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Yeast glycolytic mRNAs are differentially regulated.

et al. 1991

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The regulation of glycolytic genes in response to carbon source in the yeast Saccharomyces cerevisiae has been studied. When the relative levels of each glycolytic mRNA were compared during exponential growth on glucose or lactate, the various glycolytic mRNAs were found to be induced to differing extents by glucose. No significant differences in the stabilities of the PFK2, PGKI, PYKI, or PDCI mRNAs during growth on glucose or lactate were observed. PYK::lacZ and PGK::lacZ fusions were integrated independently into the yeast genome at the ura3 locus. The manner in which these fusions were differentially regulated in response to carbon source was similar to that of their respective wild-type loci. Therefore, the regulation of glycolytic mRNA levels is mediated at the transcriptional level. When the mRNAs are ordered with respect to the glycolytic pathway, two peaks of maximal induction are observed at phosphofructokinase and pyruvate kinase. These enzymes (i) catalyze the two essentially irreversible steps on the pathway, (ii) are the two glycolytic enzymes that are circumvented during gluconeogenesis and hence are specific to glycolysis, and (iii) are encoded by mRNAs that we have shown previously to be coregulated at the translational level in S. cerevisiae (P. A. Moore, A. J. Bettany, and A. J. P. Brown, NATO ASI Ser. Ser. H Cell Biol. 49:421-432, 1990). This differential regulation of glycolytic mRNA levels might therefore have a significant influence upon glycolytic flux in S. cerevisiae.The glycolytic pathway plays a fundamental role in the provision of metabolic energy and intermediates during fermentative growth in the yeast Saccharomyces cerevisiae. Under these conditions, the glycolytic genes are among the most efficiently expressed genes in this organism, the glycolytic enzymes comprising over 30% of soluble cell protein (for reviews, see references 20 and 70). Most yeast glycolytic genes have been isolated and sequenced (2, 4, 11, 21, 23, 25, 27, 29-31, 40, 59, 62, 63, 68, 69). The high-level expression of yeast glycolytic genes is dependent upon complex interactions between a number of cis-acting promoter elements and trans-acting transcription factors which include the RAP1, ABF1, GCR1, and GAL11 proteins (3,8,10,12,13,15,41,48,55,60,61).It is not clear whether the expression of all glycolytic genes is induced when yeast cultures are transferred from nonfermentative to fermentative carbon sources. Maitra and Lobo (37) observed 3-to 100-fold increases in the levels of glycolytic enzymes following the addition of glucose to yeast cultures growing on acetate. This work was performed on a hybrid yeast strain generated by a cross between Saccharomyces fragilis and Saccharomyces dobzhanskii (37). Some more recent studies appear to confirm this observation for S. cerevisiae. For example, analyses of the enolase (EN02), phosphoglygerate kinase (PGKJ), pyruvate kinase (PYKI), pyruvate decarboxylase (PDCI), and alcohol dehydrogenase (ADHI) mRNAs have suggested that their levels are regulated in response to ...

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Yeast glycolytic mRNAs are differentially regulated.

et al. 1991

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“…The ability of a stem-loop structure to block the progress of 40 S subunits along mRNA during "scanning" is believed to be a cause for translation inhibition in both yeast and mammalian cells (54). It has been shown that translation initiation in S. cerevisiae is very sensitive to the presence of stem-loop structures in the 5Ј-untranslated region (55,56). Therefore, the inhibitory effect of the potential rpl25-1 stemloop structure may be synergistic with absence of Cpc2.…”

Section: Discussionmentioning

confidence: 99%

Cpc2/RACK1 Is a Ribosome-associated Protein That Promotes Efficient Translation in Schizosaccharomyces pombe

Shor

Calaycay²,

Rushbrook³

et al. 2003

Journal of Biological Chemistry

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Cpc2/RACK1 is a highly conserved WD domain protein found in all eucaryotes. Cpc2/RACK1 functions on mammalian signal transduction pathways most notably as an adaptor protein for the ␤II protein kinase C isozyme. In single cell eucaryotes, Cpc2/RACK1 regulates growth, differentiation, and entry into G 0 stationary phase. The exact biochemical function of Cpc2/RACK1 is unknown. Here, we provide evidence that Cpc2 is associated with the ribosome. Using immunoaffinity purification, we isolated ribosomal proteins in association with Cpc2/ RACK1. Polysome and ribosomal subunit analysis using velocity gradient centrifugation of cell lysates demonstrated that Cpc2 co-sediments with the 40 S ribosomal subunit and with polysomes. Conditions known to disrupt ribosome structure alter sedimentation of the ribosome and of Cpc2/RACK1 coordinately. Loss of cpc2 does not dramatically alter the rate of cellular protein synthesis but causes a decrease in the steady state level of numerous proteins, some of which regulate methionine metabolism. Whereas real time PCR analysis demonstrated that transcriptional mechanisms are responsible for down-regulation of some of these proteins, one protein, ribosomal protein L25, is probably regulated at the level of translation.

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“…lB), the 4.5-kbp EcoRI-Hind111 LYS2 fragment from pUKC 3 71 (donated by Mick Tuite; University of Kent, England), the 1.1-kbp Hind111 URA3 fragment from pSPUR1 (Brown et al, 1988), and the 1.5-kbp ACTZ fragment from pSPACT9 (Bettany et al, 1989).…”

Section: Probesmentioning

confidence: 99%

The Folding of the Bifunctional TRP3 Protein in Yeast is Influenced by a Translational Pause which Lies in a Region of Structural Divergence with Escherichia coli Indoleglycerol‐Phosphate Synthase

Crombie

Boyle

Coggins

et al. 1994

European Journal of Biochemistry

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The yeast TRP3 gene encodes a bifunctional protein with anthranilate synthase I1 and indoleglycerol-phosphate synthase activities. Replacing ten consecutive non-preferred codons in the indoleglycerol-phosphate synthase region of the TRP3 gene with synonymous preferred codons (to create the TRP3pr gene ; translational pause replaced) causes a 1 .S-fold reduction in relative indoleglycerolphosphate synthase activity [Crombie, T., Swaffield, J. C. & Brown, A. J. P. (1992) J. Mol. Biol. 228,121. Here, we report that both the anthranilate synthase I1 and indoleglycerol-phosphate synthase domains are affected to similar extents when the translational pause is removed. Also, structural modelling of the yeast indoleglycerol-phosphate synthase domain against the X-ray crystal structure of indoleglycerol-phosphate synthase from Escherichia coli indicates that the translational pause lies in a region of structural divergence between similar structures. To probe the role of cytoplasmic heat-shock protein 70 (Hsp7O) chaperones in Trp3 protein folding, anthranilate synthase and indoleglycerol-phosphate synthase activities were measured in ssa and ssb mutants. Neither indoleglycerol-phosphate synthase nor anthranilate synthase were affected significantly in the ssb mutant. However, depletion of Hsp7O proteins encoded by the SSA genes led to decreased anthranilate synthase and indoleglycerol-phosphate synthase activities from the TRP3 gene, suggesting that both domains depend to some extent upon the SSA chaperone family. The data are consistent with roles for both the translational pause and Ssa chaperones in Trp3 protein folding in vivo.Detailed analyses of protein refolding in vitro have provided considerable insights into the means by which polypeptide chains attain their native three-dimensional conformation (for reviews, see Creighton, 1990;Fischer and Schmid, 1990;Kim and Baldwin, 1990;Christensen and Pain, 1991 ;Scholtz and Baldwin, 1992;Matthews, 1993). These studies have highlighted the importance of the spatial organization of amino acids within the polypeptide chain in the folding process. However, additional factors influence protein folding in vivo, including chaperones, protein disulphide isomerases and peptidyl prolyl cis-trans isomerases (for reviews, see Freedman, 1989;Fischer and Schmid, 1990;Gething and Sambrook, 1992;Hartl et al., 1992;Craig et al., 1993;Hendrick and Hartl, 1993). In addition, the temporal separation of amino acids during the synthesis of the nascent polypeptide chain might be significant for protein folding in vivo (Phillips, 1966;Baldwin, 1975;Goldberg, 1985).Previously, we proposed that distinct translational pauses have evolved in some mRNAs to promote protein folding in vivo by temporally separating the folding of specific regions of their polypeptide chains (Purvis et al., 1987). The hypothesis was based upon the following observations. (a) Nascent polypeptides start to fold as they are being synthesized (Bergman and Kuehl, 1979a;Bergman and Kuehl, 1979b;Peters and Davidson, 1982). (...

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5′‐Secondary structure formation, in constrast to a short string of non‐preferred codons, inhibits the translation of the pyruvate kinase mRNA in yeast

Cited by 45 publications

References 39 publications

Yeast glycolytic mRNAs are differentially regulated.

Yeast glycolytic mRNAs are differentially regulated.

Cpc2/RACK1 Is a Ribosome-associated Protein That Promotes Efficient Translation in Schizosaccharomyces pombe

The Folding of the Bifunctional TRP3 Protein in Yeast is Influenced by a Translational Pause which Lies in a Region of Structural Divergence with Escherichia coli Indoleglycerol‐Phosphate Synthase

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