scholarly journals Clustering of the YNA1 gene encoding a Zn(II)2Cys6 transcriptional factor in the yeast Hansenula polymorpha with the nitrate assimilation genes YNT1, YNI1 and YNR1, and its involvement in their transcriptional activation

1998 ◽  
Vol 335 (3) ◽  
pp. 647-652 ◽  
Author(s):  
Julio ÁVILA ◽  
Celedonio GONZÁLEZ ◽  
Nélida BRITO ◽  
José M. SIVERIO
Keyword(s):  
Transcriptional Activation ◽  
Hansenula Polymorpha ◽  
Nitrate Assimilation ◽  
Transcriptional Factors ◽  
Gene Encoding ◽  
Reading Frame ◽  
Transcription Start Sites ◽  
The Family ◽  
Genes Encoding ◽  
Free Media

The genes encoding the nitrate transporter (YNT1), nitrite reductase (YNI1) and nitrate reductase (YNR1) are clustered in the yeast Hansenula polymorpha. In addition, DNA sequencing of the region containing these genes demonstrated that a new open reading frame called YNA1 (yeast nitrate assimilation) was located between YNR1 and YNI1. The YNA1 gene encodes a protein of 529 residues belonging to the family of Zn(II)2Cys6 fungal transcriptional factors, and has the highest similarity to the transcriptional factors encoded by nirA, and to a smaller extent to nit-4, involved in the nitrate induction of the gene involved in the assimilation of this compound in filamentous fungi. Northern blot analysis showed the presence of the YNA1 transcript in cells incubated in nitrate, nitrate plus ammonium, ammonium, and nitrogen-free media, with a decrease in its levels in those cells incubated in ammonium. In nitrate the strain Δyna1::URA3, with a disrupted YNA1 gene, neither grew nor expressed the genes YNT1, YNI1 and YNR1. In the gene cluster YNT1-YNI1-YNA1-YNR1, the four genes were transcribed independently in the YNT1 → YNR1 direction and the transcription start sites were determined by primer extension.

scholarly journals Adenovirus E1A specifically blocks SWI/SNF-dependent transcriptional activation.

1996 ◽  
Vol 16 (10) ◽  
pp. 5737-5743 ◽  
Author(s):  
M E Miller ◽  
B R Cairns ◽  
R S Levinson ◽  
K R Yamamoto ◽  
D A Engel ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Cellular Transformation ◽  
Transcriptional Coactivator ◽  
Gene Encoding ◽  
Adenovirus E1a ◽  
Transcriptional Regulatory ◽  
Genes Encoding ◽  
Regulatory Complex ◽  
Activation Pathways ◽  
Coactivator P300

Expression of the adenovirus E1A243 oncoprotein in Saccharomyces cerevisiae produces a slow-growth phenotype with accumulation of cells in the G1 phase of the cell cycle. This effect is due to the N-terminal and CR1 domains of E1A243, which in rodent cells are involved in triggering cellular transformation and also in binding to the cellular transcriptional coactivator p300. A genetic screen was undertaken to identify genes required for the function of E1A243 in S. cerevisiae. This screen identified SNF12, a gene encoding the 73-kDa subunit of the SWI/SNF transcriptional regulatory complex. Mutation of genes encoding known members of the SWI/SNF complex also led to loss of E1A function, suggesting that the SWI/SNF complex is a target of E1A243. Moreover, expression of E1A in wild-type cells specifically blocked transcriptional activation of the INO1 and SUC2 genes, whose activation pathways are distinct but have a common requirement for the SWI/SNF complex. These data demonstrate a specific functional interaction between E1A and the SWI/SNF complex and suggest that a similar interaction takes place in rodent and human cells.

scholarly journals Dissemination of CTX-M-Type β-Lactamases among Clinical Isolates of Enterobacteriaceae in Paris, France

2004 ◽  
Vol 48 (4) ◽  
pp. 1249-1255 ◽  
Author(s):  
C. Eckert ◽  
V. Gautier ◽  
M. Saladin-Allard ◽  
N. Hidri ◽  
C. Verdet ◽  
...  
Keyword(s):  
Insertion Sequence ◽  
Dna Fingerprint ◽  
Clinical Isolates ◽  
Pcr Analysis ◽  
Reading Frame ◽  
E Coli ◽  
Paris Area ◽  
The Family ◽  
Genes Encoding ◽  
Cephalosporin Resistance

ABSTRACT We analyzed 19 clinical isolates of the family Enterobacteriaceae (16 Escherichia coli isolates and 3 Klebsiella pneumoniae isolates) collected from four different hospitals in Paris, France, from 2000 to 2002. These strains had a particular extended-spectrum cephalosporin resistance profile characterized by a higher level of resistance to cefotaxime and aztreonam than to ceftazidime. The bla CTX-M genes encoding these β-lactamases were involved in this resistance, with a predominance of bla CTX-M-15. Ten of the 19 isolates produced both TEM-1- and CTX-M-type enzymes. One strain (E. coli TN13) expressed CMY-2, TEM-1, and CTX-M-14. bla CTX-M genes were found on large plasmids. In 15 cases the same insertion sequence, ISEcp1, was located upstream of the 5′ end of the bla CTX-M gene. In one case we identified an insertion sequence designated IS26. Examination of the other three bla CTX-M genes by cloning, sequencing, and PCR analysis revealed the presence of a complex sul1-type integron that includes open reading frame ORF513, which carries the bla gene and the surrounding DNA. Five isolates had the same plasmid DNA fingerprint, suggesting clonal dissemination of CTX-M-15-producing strains in the Paris area.

scholarly journals Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?

2000 ◽  
Vol 182 (1) ◽  
pp. 143-145 ◽  
Author(s):  
Makoto Kitabatake ◽  
Man Wah So ◽  
Debra L. Tumbula ◽  
Dieter Söll
Keyword(s):  
Sulfolobus Solfataricus ◽  
Methanosarcina Barkeri ◽  
Archaeoglobus Fulgidus ◽  
Biosynthesis Pathway ◽  
Cysteine Biosynthesis ◽  
Gene Encoding ◽  
Reading Frame ◽  
Genome Data ◽  
Genes Encoding ◽  
Bacterial Genes

ABSTRACT The pathway of cysteine biosynthesis in archaea is still unexplored. Complementation of a cysteine auxotrophic Escherichia coli strain NK3 led to the isolation of the Methanosarcina barkeri cysK gene [encoding O-acetylserine (thiol)-lyase-A], which displays great similarity to bacterialcysK genes. Adjacent to cysK is an open reading frame orthologous to bacterial cysE (serine transacetylase) genes. These two genes could account for cysteine biosynthesis in this archaeon. Analysis of recent genome data revealed the presence of bacteria-like cysM genes [encodingO-acetylserine (thiol)-lyase-B] in Pyrococcusspp., Sulfolobus solfataricus, and Thermoplasma acidophilum. However, no orthologs for these genes can be found in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus, implying the existence of unrecognizable genes for the same function or a different cysteine biosynthesis pathway.

scholarly journals The carB Gene Encoding the Large Subunit of Carbamoylphosphate Synthetase from Lactococcus lactis Is Transcribed Monocistronically

1998 ◽  
Vol 180 (17) ◽  
pp. 4380-4386 ◽  
Author(s):  
Jan Martinussen ◽  
Karin Hammer
Keyword(s):  
Lactococcus Lactis ◽  
Large Subunit ◽  
Arginine Deiminase ◽  
Gene Encoding ◽  
Pyrimidine Nucleotides ◽  
Reading Frame ◽  
Glutathione Peroxidases ◽  
Carbamoylphosphate Synthetase ◽  
Genes Encoding ◽  
High Degree

ABSTRACT The biosynthesis of carbamoylphosphate is catalyzed by the heterodimeric enzyme carbamoylphosphate synthetase. The genes encoding the two subunits of this enzyme in procaryotes are normally transcribed as an operon, but the gene encoding the large subunit (carB) in Lactococcus lactis is shown to be transcribed as an isolated unit. Carbamoylphosphate is a precursor in the biosynthesis of both pyrimidine nucleotides and arginine. By mutant analysis,L. lactis is shown to possess only onecarB gene; the same gene product is thus required for both biosynthetic pathways. Furthermore, arginine may satisfy the requirement for carbamoylphosphate in pyrimidine biosynthesis through degradation by means of the arginine deiminase pathway. The expression of the carB gene is subject to regulation at the level of transcription by pyrimidines, most probably by an attenuator mechanism. Upstream of the carB gene, an open reading frame showing a high degree of similarity to those of glutathione peroxidases from other organisms was identified.

scholarly journals Interaction of Yna1 and Yna2 Is Required for Nuclear Accumulation and Transcriptional Activation of the Nitrate Assimilation Pathway in the Yeast Hansenula polymorpha

PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0135416 ◽  
Author(s):  
Lucia Silvestrini ◽  
Beatrice Rossi ◽  
Andreas Gallmetzer ◽  
Martine Mathieu ◽  
Claudio Scazzocchio ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Hansenula Polymorpha ◽  
Nitrate Assimilation ◽  
Nuclear Accumulation

scholarly journals Cloning, Expression, and Sequence Analysis of the Gene Encoding the Alkali-Stable, Thermostable Endoxylanase from Alkalophilic, Mesophilic Bacillus sp. Strain NG-27

2000 ◽  
Vol 66 (6) ◽  
pp. 2631-2635 ◽  
Author(s):  
Naveen Gupta ◽  
Vanga Shiva Reddy ◽  
Sankar Maiti ◽  
Amit Ghosh
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Active Site ◽  
Cysteine Residue ◽  
Open Reading Frame ◽  
Bacillus Sp ◽  
Gene Encoding ◽  
Reading Frame ◽  
The Family ◽  
Site Characteristic

ABSTRACT Alkalophilic Bacillus sp. strain NG-27 produces a 42-kDa endoxylanase active at 70°C and at a pH of 8.4. The gene for this endoxylanase was cloned and sequenced. The gene contained one open reading frame of 1,215 bases. An active site characteristic of the family 10 β-glycanases was recognized between amino acids 303 and 313, with the active glutamate at position 310. Though highly thermostable, the enzyme contains no cysteine residue.

scholarly journals Identification of a New Gene Essential for Germinationof Bacillus subtilis Spores withCa2+-Dipicolinate

2003 ◽  
Vol 185 (7) ◽  
pp. 2315-2329 ◽  
Author(s):  
Katerina Ragkousi ◽  
Patrick Eichenberger ◽  
Christiaan van Ooij ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Spore Germination ◽  
Function Analysis ◽  
Dipicolinic Acid ◽  
Functional Characterization ◽  
Lytic Enzyme ◽  
Spore Coat ◽  
Gene Encoding ◽  
Reading Frame ◽  
Genes Encoding

ABSTRACT Bacillus subtilis spores can germinate with a 1:1 chelate of Ca2+ and dipicolinic acid (DPA), a compound present at high levels in the spore core. Using a genetic screen to identify genes encoding proteins that are specifically involved in spore germination by Ca2+-DPA, three mutations were identified. One was in the gene encoding the cortex lytic enzyme, CwlJ, that was previously shown to be essential for spore germination by Ca2+-DPA. The other two were mapped to an open reading frame, ywdL, encoding a protein of unknown function. Analysis of ywdL expression showed that the gene is expressed during sporulation in the mother cell compartment of the sporulating cell and that its transcription is σE dependent. Functional characterization of YwdL demonstrated that it is a new spore coat protein that is essential for the presence of CwlJ in the spore coat. Assembly of YwdL itself into the spore coat is dependent on the coat morphogenetic proteins CotE and SpoIVA. However, other than lacking CwlJ, ywdL spores have no obvious defect in their spore coat. Because of the role for YwdL in a part of the spore germination process, we propose renaming ywdL as a spore germination gene, gerQ.

Cloning and sequence analysis of the hemB gene of Staphylococcus aureus

1994 ◽  
Vol 40 (8) ◽  
pp. 651-657 ◽  
Author(s):  
Badria Kafala ◽  
A. Sasarman
Keyword(s):  
Staphylococcus Aureus ◽  
Biosynthetic Pathway ◽  
Aminolevulinic Acid ◽  
Colony Growth ◽  
Reading Frame ◽  
E Coli ◽  
Preliminary Identification ◽  
The Family ◽  
Genes Encoding ◽  
Porphobilinogen Synthase

The hemB gene is a member of the family of genes encoding enzymes of the porphyrin biosynthetic pathway and codes for the enzyme porphobilinogen synthase, which is responsible for the conversion of Δ-aminolevulinic acid to porphobilinogen. To clone the hemB gene of Staphylococcus aureus we used Tn917-mediated transposon mutagenesis. Tn917 confers resistance to erythromycin and is carried by plasmid pTV1ts, which has thermosensitive replication. Hem mutants were selected by growth in the presence of kanamycin and erythromycin at 43 °C. Preliminary identification of the hem mutants was based on their dwarf colony growth, which could be restored to normal by hemin. DNA extracted from one of the hem mutants was digested with several restriction endonucleases and hybridized to a probe representing the XbaI–AvaI end of Tn917. A BglII–EcoRI fragment of 4.5 kb gave a positive signal and was cloned into pUC18. Transformants were identified by colony hybridization with the Tn917 probe. The positive clones were sequenced, starting from the transposon end. The results allowed us to identify an open reading frame whose nucleotide sequence presented a homology of 63% to the sequence of the hemB gene of Bacillus subtilis and of 55% to the sequence of the hemB gene of Escherichia coli K12. No other nucleotide sequences, except those belonging to known hemB genes, presented significant homologies to our sequence. The cloning of the hemB gene of S. aureus was confirmed by the ability of the gene to complement a hemB mutant of E. coli K12. To our knowledge, this is the first report of the cloning of a hem gene in S. aureus.Key words: Δ-aminolevulinic acid dehydratase, hemB gene, S. aureus, heme, porphyrins.

Molecular Physiology and Pathophysiology of Electroneutral Cation-Chloride Cotransporters

2005 ◽  
Vol 85 (2) ◽  
pp. 423-493 ◽  
Author(s):  
Gerardo Gamba
Keyword(s):  
Cell Volume Regulation ◽  
Molecular Physiology ◽  
Gene Encoding ◽  
Ion Absorption ◽  
The Family ◽  
Genes Encoding ◽  
Potential Equilibrium ◽  
Cation Chloride Cotransporters ◽  
Inactivating Mutations ◽  
Made In

Electroneutral cation-Cl−cotransporters compose a family of solute carriers in which cation (Na+or K+) movement through the plasma membrane is always accompanied by Cl−in a 1:1 stoichiometry. Seven well-characterized members include one gene encoding the thiazide-sensitive Na+−Cl−cotransporter, two genes encoding loop diuretic-sensitive Na+−K+−2Cl−cotransporters, and four genes encoding K+−Cl−cotransporters. These membrane proteins are involved in several physiological activities including transepithelial ion absorption and secretion, cell volume regulation, and setting intracellular Cl−concentration below or above its electrochemical potential equilibrium. In addition, members of this family play an important role in cardiovascular and neuronal pharmacology and pathophysiology. Some of these cotransporters serve as targets for loop diuretics and thiazide-type diuretics, which are among the most commonly prescribed drugs in the world, and inactivating mutations of three members of the family cause inherited diseases such as Bartter's, Gitelman's, and Anderman's diseases. Major advances have been made in the past decade as consequences of molecular identification of all members in this family. This work is a comprehensive review of the knowledge that has evolved in this area and includes molecular biology of each gene, functional properties of identified cotransporters, structure-function relationships, and physiological and pathophysiological roles of each cotransporter.

scholarly journals Distribution of the Water-Soluble Astaxanthin Binding Carotenoprotein (AstaP) in Scenedesmaceae

Marine Drugs ◽  
2021 ◽  
Vol 19 (6) ◽  
pp. 349
Author(s):  
Hiroki Toyoshima ◽  
Ami Miyata ◽  
Risako Yoshida ◽  
Taichiro Ishige ◽  
Shinichi Takaichi ◽  
...  
Keyword(s):  
Water Soluble ◽  
Stress Conditions ◽  
Soluble Form ◽  
Light Conditions ◽  
Photooxidative Stress ◽  
Gene Encoding ◽  
Chlorella Variabilis ◽  
Cell Extracts ◽  
The Family ◽  
Genes Encoding

Photooxidative stress-inducible water-soluble astaxanthin-binding proteins, designated as AstaP, were identified in two Scenedesmaceae strains, Coelastrella astaxanthina Ki-4 and Scenedesmus obtusus Oki-4N; both strains were isolated under high light conditions. These AstaPs are classified as a novel family of carotenoprotein and are useful for providing valuable astaxanthin in water-soluble form; however, the distribution of AstaP orthologs in other microalgae remains unknown. Here, we examined the distribution of AstaP orthologs in the family Scenedesmaceae with two model microalgae, Chlamydomonas reinhardtii and Chlorella variabilis. The expression of AstaP orthologs under photooxidative stress conditions was detected in cell extracts of Scenedesmaceae strains, but not in model algal strains. Aqueous orange proteins produced by Scenedesmaceae strains were shown to bind astaxanthin. The protein from Scenedesmus costatus SAG 46.88 was purified. It was named ScosAstaP and found to bind astaxanthin. The deduced amino acid sequence from a gene encoding ScosAstaP showed 62% identity to Ki-4 AstaP. The expression of the genes encoding AstaP orthologs was shown to be inducible under photooxidative stress conditions; however, the production amounts of AstaP orthologs were estimated to be approximately 5 to 10 times lower than that of Ki-4 and Oki-4N.

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