Filter replicas and permanent collections of recombinant DNA plasmids

Gergen, J. Peter; Stern, Robert L.; Wensink, Pieter C.

doi:10.1093/nar/7.8.2115

Cited by 351 publications

(177 citation statements)

References 36 publications

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“…CRY) cDNA clones were isolated from a yeast cDNA library constructed and kindly supplied by Gary McKnight (45). The 32P-labeled EcoRI-BglII fragment from CRY) was used as a probe for colony hybridization (17) to approximately 20,000 colonies from the library. Plasmid DNAs were isolated from positive colonies and were screened by restriction enzyme mapping for those preparations containing CRY) cDNAs.…”

Section: Methodsmentioning

confidence: 99%

Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene.

Larkin¹,

Thompson²,

Woolford³

1987

Mol. Cell. Biol.

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The Saccharomyces cerevisiae CRY] gene encodes ribosomal protein rp59, a component of the 40S ribosomal subunit. Mutations in CRY] can confer resistance to the alkaloid cryptopleurine, an inhibitor of the elongation step of translation. The nucleotide sequence of the cloned CRY] gene was determined. The predicted amino acid sequence shows that CRY] encodes a 14,561-dalton polypeptide that has 88% amino acid sequence homology to the hamster or human S14 ribosomal protein responsible for emetine resistance and 45% homology to Escherichia coli ribosomal protein Sll. Analysis of the DNA sequences upstream from CRYI revealed the presence of three sequences, HOMOLl (consensus, A/TACATCC/TG/ATA/GCA), RPG (consensus, ACCCA/ GTACATT/CT/A), and a thymine-rich sequence, found upstream of more than 20 other cloned yeast genes encoding components of the translational apparatus. We exploited the ability to assay the expression of CRY) in vivo by using the cryptopleurine resistance phenotype to demonstrate that these three consensus sequences are necessary for the transcription of CRY). We previously showed that the upstream promoter element of the yeast RP39A gene consists of these identical sequence motifs. Therefore, we suggest that these three sequences define a consensus promoter element for the genes encoding the yeast translational apparatus. CRY) is one of several hundred yeast genes, including ribosomal protein genes, whose expression is transiently decreased 10-fold upon heat shock. We found that the HOMOLl and RPG consensus sequences are not necessary for the heat shock response of CRY).The biosynthesis, assembly, and function of ribosomes are complicated interrelated processes essential to the function and growth of all cells. Equimolar quantities of more than 70 different ribosomal proteins synthesized in the cytoplasm and four ribosomal RNAs transcribed in the nucleus are assembled into ribosomes in the nucleolus (16). Ribosome biosynthesis is tightly coordinated with the physiological state of the cells. In the yeast Saccharomyces cerevisiae, the rate of synthesis of ribosomal proteins is coordinately decreased in response to heat shock (31) or upon sporulation (33) and is increased when the yeast is shifted from medium containing ethanol as a carbon source to medium containing glucose as a carbon source (29). To study the coordinate expression of ribosomal genes and the role of individual ribosomal components in yeast ribosome assembly and function, we and other workers have cloned a number of yeast ribosomal protein genes (4, 5, 13-15, 22, 35, 37, 39, 60, 72). With few exceptions, these genes are unlinked, occur in two copies in the genome, and contain a single intervening sequence (1, 4, 5, 13-16, 28, 35, 48, 72, 73).Experiments thus far indicate that a variety of control mechanisms operate to coordinate yeast ribosome biosynthesis. Ribosomal protein mRNA transcription, processing, stability, and translation are regulated, as well as the stability of the ribosomal proteins themselves (11, 12, 18, 19, 29-31,...

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Section: Methodsmentioning

confidence: 99%

Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene.

Larkin¹,

Thompson²,

Woolford³

1987

Mol. Cell. Biol.

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“…To obtain the initial $14 cDNA clones, a 2.2-kb HindIII fragment containing the Saccharomyces cerevisiae CRY1 gene (Larkin and Woolford 1983) was used as a probe to screen the BMS cDNA library by the colony hybridization procedure of Gergen et al (1979) under low stringency hybridization conditions (20% formamide, 6x SSPE, 1 x Denhardt's solution, 0.1% SDS, 0.1 mg/ml calf thymus DNA, 20 ~g/ml poly(A) at 35~ and washed four times for 15 min each with 2 x SSPE, 0.2% SDS at 45~ [1 x SSPE is 0.15 M NaC1, 0.01 M NaH2PO4, 8 mM NaOH, 1 mavi Na~EDTA (pH 7.0), 1 x Denhardt's solution is 0.02% each of bovine serum albumin, Ficoll, and polyvinyl pyrrolidone]. These hybridization conditions were modified from those of Howley et al (1979).…”

Section: Isolation and Analysis Of Cdna Clonesmentioning

confidence: 99%

The organization and expression of a maize ribosomal protein gene family.

Larkin¹,

Hunsperger

Culley

et al. 1989

Genes Dev.

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We have isolated several Zea mays cDNAs encoding the 40S subunit ribosomal protein S14. In maize, this ribosomal protein is encoded by a small multigene family, at least three members of which are expressed. S14 transcript levels are highest in mitotically active tissues, such as seedling shoot, developing endosperm, and tassel primordia, and lowest in tissues with little cell division, such as mature leaf and root. Very little S14 RNA is present in pollen, suggesting that translation of pollen mRNAs during pollen germination uses preformed ribosomes. During kernel development, the highest levels of S14 transcripts in endosperm tissue are found at 10-12 days postpollination; S14 RNA levels decline continuously from this point onward. The period of maximal expression of the S14 ribosomal protein gene appears to precede the onset of storage protein synthesis and does not correlate with the reported times of increased nucleolar volume or genome amplification.

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“…(13) . Radiolabeled probes from tau or total mRNA were made by using reverse transcriptase in first strand synthesis with [a-"P]deoxycytosine triphosphate .…”

Section: Isolation and Characterization Of Tau Cdna Clonesmentioning

confidence: 99%

Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes.

Drubin¹,

Caput²,

Kirschner³

1984

The Journal of Cell Biology

164

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Tau protein is a collection of closely related polypeptides that associate with microtubules in vivo and stimulate their assembly in vitro. Using an affinity-purified antiserum against bovine brain tau protein, we found that the number and amount of tau polypeptides changes dramatically during mouse brain development. The different forms appear to result from changes in tau mRNA since in vitro translation products reflect the qualitative and quantitative changes found in vivo. To study the mRNA and genomic complexity of tau protein, we used tau mRNA, purified from polysomes with tau antiserum, to isolate embryonic mouse tau complementary DNA clones. With these probes we have determined that embryonic tau protein is translated from a 6-kb mRNA that persists throughout brain development.

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Filter replicas and permanent collections of recombinant DNA plasmids

Cited by 351 publications

References 36 publications

Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene.

Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene.

The organization and expression of a maize ribosomal protein gene family.

Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes.

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