[73] Zinc-containing cyclic nucleotide phosphodiesterases from bakers' yeast

Londesborough, John; Suoranta, K

doi:10.1016/0076-6879(88)59075-4

Cited by 16 publications

(24 citation statements)

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“…It encodes a high-affinity cyclic AMP (cAMP) phosphodiesterase (32,34). In this report, we describe another such gene, PDEI, which encodes a lowaffinity cAMP phosphodiesterase (21). We have examined the phenotype caused by disruption of the PDE genes and have found that PDEI does not appear to have any essential function.…”

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confidence: 99%

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

1987

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Saccharomyces cerevisiae contains two genes which encode cyclic AMP (cAMP) phosphodiesterases. We previously isolated and characterized PDE2, which encodes a high-affinity cAMP phosphodiesterase. We have now isolated the PDEI gene of S. cerevisiae, which encodes a low-affinity cAMP phosphodiesterase. These two genes represent highly divergent branches in the evolution of phosphodiesterases. High-copy-number plasmids containing either PDEI or PDE2 can reverse the growth arrest defects of yeast cells carrying the jRA2Val19 mutation. PDEI and PDE2 appear to account for the aggregate cAMP phosphodiesterase activity of S.cerevisiae. Disruption of both PDE genes results in a phenotype which resembles that induced by the RAu2Val-19 mutation. pdel-pde2-rasl-ras2-cells are viable.We have been investigating the pathways of growth regulation in the yeast Saccharomyces cerevisiae, particularly those pathways which involve the RAS proteins. The RAS] and RAS2 genes of S. cerevisiae are structurally and functionally closely related to the mammalian ras oncogenes (10,11,17,29). In S. cerevisiae, RAS proteins modulate adenylate cyclase in a GTP-dependent manner (4, 37). Yeast cells have severe defects in growth control when they lack RAS genes or contain RAS2 mutations analogous to those which activate the oncogenic properties of the mammalian RAS genes (18,35). In particular, yeast cells containing the

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confidence: 99%

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

1987

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“…According to the hypothesis, V. fischeri cells in the animal light organ elicit the overproduction and release of host cAMP by secreting a toxin that, through an ADP-ribosylating activity, interferes with the regulation of host adenyl ate cyclase in a manner analogous to the secretion and activity of cholera enterotoxin by V. cholerae in the human intestine (6,7,35). Recent evidence indicating that V. fischeri contains torRS genes (36) is consistent with this hypothesis.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, MJ-l is brightly luminescent in laboratory culture, whereas ES 114 and its derivatives are not visibly luminescent under the same conditions [35]. The qsrP gene was isolated from ESRI by PCR-amplification of the relevant chromosomal DNA using To determine if QsrP is involved in the symbiotic relationship between V. fischeri and its invertebrate host E. scolopes, ES-lOX was used both alone and in competition with the parent strain in squid colonization assays (Materials and Methods).…”

Section: Dunlap Unpublished Data)mentioning

confidence: 99%

“…In the early 1970's it became evident that the production of light by V. fischeri is regulated by a small diffusable extracellular signal that accumulated in the medium when cells reached high population density [34,35]. Culture media that had been "conditioned" by the growth of V. fischeri to early stationary phase could be used to stimulate the luminescence of early exponential phase cultures, which provided an assay for the signal molecule.…”

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confidence: 99%

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The quorum-sensing regulation of Vibrio fischeri : novel components of the autoinducer/LuxR regulatory circuit

Callahan¹

1999

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In the marine bacterium Vibrio fischeri two intercellular homoserine-Iactone signal molecules (luxI-dependent 30C 6 -HSL and the ainS-dependent Cs-HSL) and the transcriptional activator LuxR regulate the luminescence system in a cell-density dependent manner by a process termed quorum sensing. In this study, five additional proteins whose production is regulated by quorum sensing are described, and the genes encoding four of the five proteins, denoted as QsrP, RibB, QsrV, and AcfA, are analyzed. Each protein is positively regulated by 30C 6 -HSL and LuxR and negatively regulated at low population density by Cs-HSL. Probable LuxRlautoinducer binding sites are found in the promoter region of each. QsrP and RibB are encoded monocistronically, whereas AcfA and QsrV appear to be encoded by a two-gene operon. On the basis of sequence similarity to proteins of known function from other organisms, RibB is believed to be an enzyme that catalyzes the transformation of ribulose 5-phosphate to 3,4-dihydroxy-2-butanone 4-phosphate, a precursor for the xylene ring of riboflavin; AcfA is believed to be a pilus subunit; and the functions of QsrP and QsrV are unknown at this time. A qsrP mutant was reduced in its ability to colonize its symbiotic partner, Euprymna scolopes when placed in competition with the parent strain. On the other hand, a mutant strain of V. fischeri containing an insertion in acfA, which is believed to be polar with respect to qsrV, displayed enhanced colonization competence in a competition assay. A ribB mutant grew well on media not supplemented with additional riboflavin and displayed normal induction of luminescence. Both phenotypes suggest that the lack of a functional ribB gene is complemented by another gene of similar function in the mutant. Oriented divergently from acfA are open reading frames that code for two putative proteins that are similar in sequence to members of the LysR family of transcriptional regulators. Organization of the two divergent sets of genes and the shared promoter region suggests that transcription of acfA and qsrV may be regulated by one or both of these divergently transcribed proteins. This work defines a quorum-sensing regulon in V. fischeri. A model describing its regulation is presented.2

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“…cerevisiae contains two known cAMP phosphodiesterases, a high-Km enzyme with broad specificity and a low-Km enzyme with narrow specificity (20,28). For this report, we cloned, sequenced, and mapped SRA5.…”

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SRA5 encodes the low-Km cyclic AMP phosphodiesterase of Saccharomyces cerevisiae.

Wilson¹,

Tatchell²

1988

Mol. Cell. Biol.

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sraS mutations in Saccharomyces cerevisiae were previously shown to suppress the inefficient growth of ras2 strains on nonfermentable carbon sources and to result in deficient low-Km, cyclic AMP (cAMP) phosphodiesterase activity. We have cloned SRA5 by complementation. It maps to the right arm of chromosome XV, tightly linked to PRT(, and its sequence matches the sequence of PDE2, encoding the low-Km cAMP phosphodiesterase. Disruptions of SRAS allowed rasl ras2 strains to grow either on rich media supplemented with cAMP or on minimal media without exogenous cAMP. sra5 strains failed to survive prolonged nitrogen starvation in the presence of exogenous cAMP.The yeast Saccharomyces cerevisiae contains two genes, RAS] and RAS2, that are structurally and functionally homologous to the ras oncogenes of mammalian cells (9,10,17,24). RAS gene products bind guanine nucleotides and have intrinsic GTPase activity (for reviews, see references 1 and 13). Biochemical and genetic evidence indicates that, in S. cerevisiae, RAS gene products activate adenylate cyclase (5-7, 16, 17, 32 (4,6,11,30). SRA1 encodes the regulatory subunit of the cyclic AMP (cAMP)-dependent protein kinase, and SRA3 encodes one of the catalytic subunits (7). Dominant SRA4 mutations map to the cyri (adenylate cyclase) locus and result in high constitutive levels of RAS-independent adenylate cyclase activity (6). Mutations in SRA6 result in derepressed RAS] transcription (4), and mutations in SRA5 result in deficient low-Km cAMP phosphodiesterase activity (6).S. cerevisiae contains two known cAMP phosphodiesterases, a high-Km enzyme with broad specificity and a low-Km enzyme with narrow specificity (20,28). For this report, we cloned, sequenced, and mapped SRA5. We demonstrate by sequence homology that SRA5 encodes the low-Km cAMP phosphodiesterase of S. cerevisiae, and we describe some of the phenotypic consequences of its disruption.Cloning of ,fA5. The wild-type SRA5 gene was cloned by virtue of its ability to rescue a RAS' sraS-5 strain from dying upon nitrogen starvation in the presence of exogenous cAMP. Th; strain RW60-12C (RAS' sraS-5) was transformeO (2) ywith a yeast genomic library constructed in the ments all phenotypes of sra5-3 and sra5-5 previously described (6). Subcloning (21) and TnS mutagenesis (27) further delineated the location of the functional gene ( Fig. la and b).A URA3 gene was integrated at the pWl-insert chromosomal locus by transforming RW58 (ras2::LEU2 ura3) with pW4, an integrating plasmid containing URA3 and a functional portion of the pWl insert (Tables 1 and 2; Fig. 1). A stable Ura+ (Sra5S) transformant (RW158) was crossed with RW77 (ras2::LEU2 sraS-3 ura3); the segregation pattern of URA3 and sraS-3 was 27 parental ditype:0 nonparental ditype:0 tetratype. This linkage (less than 2 centimorgans) between the pWl insert locus and the sra5-3 locus indicates that the pWl insert contains SRA5 and not an extragenic suppressor thereof.Mapping of SRAS to chromosome XV. Preliminary assignment of SRA5 to chromosome VII or XV wa...

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[73] Zinc-containing cyclic nucleotide phosphodiesterases from bakers' yeast

Cited by 16 publications

References 9 publications

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

The quorum-sensing regulation of Vibrio fischeri : novel components of the autoinducer/LuxR regulatory circuit

SRA5 encodes the low-Km cyclic AMP phosphodiesterase of Saccharomyces cerevisiae.

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