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4 edition of Identification of an upstream activating sequence of the yeast pyruvate kinase gene (PYK) found in the catalog.

Identification of an upstream activating sequence of the yeast pyruvate kinase gene (PYK)

Philip Dykshoorn

Identification of an upstream activating sequence of the yeast pyruvate kinase gene (PYK)

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Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

SeriesCanadian theses = Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches.
ID Numbers
Open LibraryOL18682097M
ISBN 100315565691
OCLC/WorldCa24907016

The glycolysis pathway is nearly universal in biological systems. Glycolysis is the sequence of reactions that converts glucose to pyruvate with the concomitant formation of ATP. Three fates of this pyruvate produced exist. In this practical the production of pyruvate and . Skip to main content. UFDC Home | UF Institutional Repository | | UF Institutional Repository |. As well as allosterically activating the enzyme by up to 5-fold, 9 AMP also promotes its phosphorylation 11 at a specific threonine residue on the α subunit (Thr 12) by an upstream kinase that has recently been identified as a complex between the tumor suppressor protein LKB1 and 2 accessory subunits, termed STRAD and MO 13, Abstract. A scheme for the preparation of pyruvate kinase (EC ) in gram amounts from yeast is described which utilizes two (NH 4) 2 SO 4 fractionations followed by successive chromatography on DEAE-cellulose and cellulose phosphate columns in 50% aqueous glycerol. The resulting enzyme had a specific activity of µmoles per min per mg at 30°.


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Identification of an upstream activating sequence of the yeast pyruvate kinase gene (PYK) by Philip Dykshoorn Download PDF EPUB FB2

Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae. M Nishizawa Biosciences Laboratory, Mitsubishi Kasei Corporation, Yokohama, by: Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

M Nishizawa, R Araki, and Y Teranishi Biosciences Laboratory, Mitsubishi Kasei Corporation, Yokohama, by:   Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

Mol Cell Biol. Feb; 9 (2)– [PMC free article] Vignais ML, Woudt LP, Wassenaar GM, Mager WH, Sentenac A, Planta by: T1 - Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

AU - Nishizawa, M. AU - Araki, R. AU - Teranishi, Y. PY - /2. Y1 - /2Cited by: Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

Mol Cell Biol. Feb; 9 (2)– [PMC free article] Ogden JE, Stanway C, Kim S, Mellor J, Kingsman AJ, Kingsman by:   Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

Mol Cell Biol. Feb; 9 (2)– [PMC free article]. The DNA-binding protein RAP1 is required for efficient transcriptional activation of the yeast PYK glycolytic gene. Curr Genet. Dec; 18 (5)– Nishizawa M, Araki R, Teranishi Y.

Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae. Nishizawa, M., Araki, R. and Teranishi, Y. () Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

9: – PubMed Google Scholar. 5' AMP-activated protein kinase or AMPK or 5' adenosine monophosphate-activated protein kinase is an enzyme (EC ) that plays a role in cellular energy homeostasis, largely to activate glucose and fatty acid uptake and oxidation when cellular energy is low.

It belongs to a highly conserved eukaryotic protein family and its orthologues are SNF1 in yeast, and SnRK1 in plants. Expression of the yeast phosphoglycerate kinase gene (PGK) requires the binding of RAP1 to the activator core sequence within the upstream activating sequence (UAS) of PGK.

Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

Mol Cell Biol. Feb; 9 (2)– [PMC free article] Siliciano PG, Tatchell K. Transcription and regulatory signals at the mating type locus in yeast.

M Nishizawa, R Araki, Y TeranishiIdentification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae Mol.

Cell. Biol., 9 (), pp. To clarify carbon source-dependent control of the glycolytic pathway in the yeast Saccharomyces cerevisiae, we have initiated a study of transcriptional regulation of the pyruvate kinase gene (PYK).

By deletion analysis of the 5'-noncoding region of the PYK gene, we have identified an upstream activating sequence (UASPYK1) located between A yeast two-hybrid assay investigates protein–protein interactions by exploiting a transcription system normally used by yeast cells.

In a normal yeast cell, a transcription factor called Gal4 binds to a promoter region called an upstream activating sequence (UAS). Gal4 is composed of a binding domain (BD), which binds to the UAS, as well as. Yeast pyruvate kinase *, PK, was first purified from bakers’ yeast by Washio et al.

1, 2 in and obtained in pure form from brewers’ yeast by Hess et al. 3 and Hunsley and Suelter ymes of pyruvate kinase do not occur in yeast. The values for the molecular weight vary between 4 (determined with the ultracentrifuge), 3 (calculated from the amino acid. In the yeast Saccharomyces cerevisiae, fermentation is the major pathway for energy production, even under aerobic conditions.

However, when glucose becomes scarce, ethanol produced during fermentation is used as a carbon source, requiring a shift to respiration. This adaptation results in massive reprogramming of gene expression.

Increased expression of genes for gluconeogenesis and. We show by deletion mutagenesis, followed by in vivo and in vitro analysis, that the binding of a protein factor to the upstream activation sequence (USA) of the Saccharomyces cerevisiae glycolytic gene PYK, encoding pyruvate kinase, is required for efficient transcription of the corresponding coding region.

In addition, gel electrophoretic mobility shift and DNase I protection studies. Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae. Mol Cell Biol. Feb; 9 (2)– Thepromoter ofthe yeast glycolytic gene encoding phosphoglycerate kinase (PGK) contains an upstream activation sequence between bases and upstream ofthe initiating upstream activation.

Abstract. The kinetic properties of purified yeast pyruvate kinase were investigated. The enzyme showed cooperative kinetics toward the essential activating monovalent cations K + and NH 4 +, Mg 2+, and se 1,6-diphosphate, which yielded homotropic cooperative kinetics and did not affect maximal velocity, transformed the sigmoidal kinetics of K + and NH 4 +, Mg 2+, and.

activated protein kinase-activated protein kinase 2 (MK2 or MAPKAPK2), budding uninhibited by benzimidazoles 1 homo - log (yeast) (BUB1), pyruvate kinase, liver and RBC (PKLR), never in mitosis gene A-related kinase 4 (NEK4), protein kinase C and casein kinase substrate in.

To understand the diversity of transcripts in yeast (Saccharomyces cerevisiae) we analyzed the transcriptional landscapes for cells grown under 18 different environmental conditions. Each sample was analyzed using RNA-sequencing, and a total ofuniquely mapped reads andpoly-adenylated end tags were produced.

Consistent with previous studies, we find that the majority of. Schematic representation of transcription of the pyruvate kinase L and M genes. In the pyruvate kinase type L gene (A), the exons specific for type L and R are indicated by hatched and solid boxes, respectively.

In the pyruvate kinase type M gene (B), the exons specific for type M1 and M2 are indicated by hatched and solid boxes, respectively.

Escherichia coli contains 30 two-component systems (TCSs), each consisting of a histidine kinase and a response regulator.

Whereas most TCSs are well characterized in this model organism, little is known about the YpdA/YpdB system. To identify YpdB-regulated genes, we compared the transcriptomes of E.

coli cells overproducing either YpdB or a control protein. Pyruvate kinases from a variety of sources including brewers’ yeast, rat and mouse liver, and rat adipose tissue (14) have been shown to exhibit sigmoidal kinetics and activation by fructose 1,6-diphosphate.

The homogeneous bakers’ yeast pyruvate kinase preparation of Hunsley and Suelter (5). Abstract. The UAS of the yeast gene encoding the glycolytic enzyme phosphoglycerate kinase (PGK) contains several different sequence elements involved in transcriptional elements include the activator core sequence, which is bound by the RAP1 protein, and three copies of the pentamer sequence 5′ CTTCC 3′.

For example, conversion of phosphoenolpyruvic acid to pyruvate, the final common step of glycolysis, is mediated by the enzyme pyruvate kinase (PK), which is coded for by two separate genes.

The PKL and PKR isoforms are splice variants of the first gene and are expressed exclusively in the liver and red blood cells, respectively. Nishizawa M, Araki R, Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae.

Mol Cell Biol. Feb; 9 (2)– [PMC free article] Chambers A, Tsang JS, Stanway C, Kingsman AJ, Kingsman SM. The UAS of the yeast gene encoding the glycolytic enzyme phosphoglycerate kinase (PGK) contains several different sequence elements involved in transcriptional activation.

Activation of Yeast Pymvate Kinase Vol.No. 19 TABLE I JCffect of vaGous conditions on Ii, and Hill slope (nH) for P-enolpyruvate saturulion kinetics Yeast pyruvate kinase was assayed as previously described (10) at 5 IBM ADP, 17 IIIM MgCl, 11 KCl, varying P-enolpyru.

GO ID GO Aspect Cellular Component Description Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).

phosphoglycerate kinase (PGK) is a strong yeast promoter (1). It contains an upstream activation sequence (UAS) located betweenbases and upstream fromthe initiating ATG. This is in contrast with synthetic media for which nitrogen sources were in excess.

A second explanation in the case of PYK1 deletion is FPYK1 was hemizygous for that deletion (PYK1 is an essential yeast gene). The maximal reduction in pyruvate kinase activity we would expect from this construction is 50 %.

In contrast, Pierce et al. used a. A gene encoding pyruvate carboxylase has previously been isolated from Saccharomyces cerevisiae. We have isolated a second gene, PYC2, from the same organism also encoding a pyruvate carboxylase.

The gene PYC2 is situated on the right arm of chromosome II between the DUR 1, 2 markers and the telomere. We localized the previously isolated gene, which we designate PYC1, to chromosome VII.

The gene activation networks are still poorly understood. In order to address the involved protein–DNA and protein–protein interactions, a number of methods have been developed that efficiently address cis-element interacting partners. This chapter describes two powerful methods: the yeast one-hybrid system and the yeast two-hybrid system.

An Arabidopsis SOS2 (salt overly sensitive 2)-like protein kinase gene, PKS6, was expressed in leaves, stems, and siliques, but not detectable in roots of adult plants; its expression in young seedlings was up-regulated by abscisic acid.

To determine the biochemical properties of the PKS6 protein, we expressed the PKS6 coding sequence as a glutathione S-transferase fusion protein in. Mitogen Activated Protein (MAP) kinase kinase kinase, MAPKKK (or MAP3K) is a serine/threonine-specific protein kinase which acts upon MAP kinase uently, MAP kinase kinase activates MAP kinase.

Several types of MAPKKK can exist but are mainly characterized by the MAP kinases they activate. The complete amino acid sequence of cat muscle pyruvate kinase has been determined and fitted to the A resolution electron density map. catalysed by yeast pyruvate kinase when activated by.

proposed benzylsuccinate synthase-activating enzyme have also been cloned from T. aromatica K and T. aromatica T1 and designated bssD and tutE, respectively (8, 19).

The pro-posed function is based on the similarities of these gene prod-ucts with pyruvate formate-lyase-activating enzymes (8, 19). The bssD and tutE genes are located upstream. Gene. In humans, the TP53 gene is located on the short arm of chromosome 17 (17p).

The gene spans 20 kb, with a non-coding exon 1 and a very long first intron of 10 kb. The coding sequence contains five regions showing a high degree of conservation in vertebrates, predominantly in exons 2, 5, 6, 7 and 8, but the sequences found in invertebrates show only distant resemblance to mammalian.

Pyruvate decarboxylase, PDCase, activity in wild-type yeast cells growing on ethanol is quite low but increases up to tenfold upon addition of glucose, less with galactose and only slightly with glycerol.

PDCase levels in glycolysis mutant strains growing on ethanol or acetate were higher than in the wild-type strain. These levels correlated with the sum of the concentrations of three-carbon.A mitogen-activated protein kinase (MAPK or MAP kinase) is a type of protein kinase that is specific to the amino acids serine and threonine (i.e., a serine/threonine-specific protein kinase).MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory regulate cell functions including.Telomerase is an RNA-directed DNA polymerase, composed of RNA and protein subunits, that replicates the telomere ends of linear eukaryotic chromosomes.

Using a genetic strategy described here, we identify the product of the EST2 gene, Est2p, as a subunit of telomerase in the yeast Saccharomyces cerevisiae.

Est2p is required for enzyme catalysis, as mutations in EST2 were found to result in.