Autoregulation of the Kluyveromyces lactis pyruvate decarboxylase gene KlPDC1 involves the regulatory gene RAG3

In the yeast Kluyveromyces lactis, the pyruvate decarboxylase gene KlPDC1 is strongly regulated at the transcription level by different environmental factors. Sugars and hypoxia act as inducers of transcription, while ethanol acts as a repressor. Their effects are mediated by gene products, some of which have been characterized. KlPDC1 transcription is also strongly repressed by its product – KlPdc1 – through a mechanism called autoregulation. We performed a genetic screen that allowed us to select and identify the regulatory gene RAG3 as a major factor in the transcriptional activity of the KlPDC1 promoter in the absence of the KlPdc1 protein, i.e. in the autoregulatory mechanism. We also showed that the two proteins Rag3 and KlPdc1 interact, co-localize in the cell and that KlPdc1 may control Rag3 nuclear localization.

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RAG3 gene and transcriptional regulation of the pyruvate decarboxylase gene in Kluyveromyces lactis

Molecular Microbiology ◽

10.1111/j.1365-2958.1996.tb02515.x ◽

1996 ◽

Vol 20 (4) ◽

pp. 765-772 ◽

Cited By ~ 22

Author(s):

C. Prior ◽

L. Tizzani ◽

H. Fukuhara ◽

M. Wésolowski-Louvel

Keyword(s):

Transcriptional Regulation ◽

Kluyveromyces Lactis ◽

Pyruvate Decarboxylase

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Tyrosine phosphorylation controls nuclear localization and transcriptional activity of Ssdp1 in mammalian cells

Journal of Cellular Biochemistry ◽

10.1002/jcb.21576 ◽

2008 ◽

Vol 103 (6) ◽

pp. 1856-1865 ◽

Cited By ~ 1

Author(s):

Ipsita Dey-Guha ◽

Nasir Malik ◽

Renaud Lesourne ◽

Paul E. Love ◽

Heiner Westphal

Keyword(s):

Tyrosine Phosphorylation ◽

Nuclear Localization ◽

Mammalian Cells ◽

Transcriptional Activity

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A Genetic Screen for Suppressors and Enhancers of the Drosophila Cdk1-Cyclin B Identifies Maternal Factors That Regulate Microtubule and Microfilament Stability

Genetics ◽

10.1093/genetics/162.3.1179 ◽

2002 ◽

Vol 162 (3) ◽

pp. 1179-1195 ◽

Cited By ~ 3

Author(s):

Jun-Yuan Ji ◽

Marjan Haghnia ◽

Cory Trusty ◽

Lawrence S B Goldstein ◽

Gerold Schubiger

Keyword(s):

Cell Cycle ◽

Cell Cycle Progression ◽

Genetic Screen ◽

Cyclin B ◽

Gene Products ◽

Nuclear Movement ◽

Cell Cycles ◽

Major Mechanism ◽

Cytoskeletal Dynamics ◽

Chromosome Bridges

Abstract Coordination between cell-cycle progression and cytoskeletal dynamics is important for faithful transmission of genetic information. In early Drosophila embryos, increasing maternal cyclin B leads to higher Cdk1-CycB activity, shorter microtubules, and slower nuclear movement during cycles 5-7 and delays in nuclear migration to the cortex at cycle 10. Later during cycle 14 interphase of six cycB embryos, we observed patches of mitotic nuclei, chromosome bridges, abnormal nuclear distribution, and small and large nuclei. These phenotypes indicate disrupted coordination between the cell-cycle machinery and cytoskeletal function. Using these sensitized phenotypes, we performed a dosage-sensitive genetic screen to identify maternal proteins involved in this process. We identified 10 suppressors classified into three groups: (1) gene products regulating Cdk1 activities, cdk1 and cyclin A; (2) gene products interacting with both microtubules and microfilaments, Actin-related protein 87C; and (3) gene products interacting with microfilaments, chickadee, diaphanous, Cdc42, quail, spaghetti-squash, zipper, and scrambled. Interestingly, most of the suppressors that rescue the astral microtubule phenotype also reduce Cdk1-CycB activities and are microfilament-related genes. This suggests that the major mechanism of suppression relies on the interactions among Cdk1-CycB, microtubule, and microfilament networks. Our results indicate that the balance among these different components is vital for normal early cell cycles and for embryonic development. Our observations also indicate that microtubules and cortical microfilaments antagonize each other during the preblastoderm stage.

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Dimerization through the helix-loop-helix motif enhances phosphorylation of the transcription activation domains of myogenin

Molecular and Cellular Biology ◽

10.1128/mcb.14.9.6232-6243.1994 ◽

1994 ◽

Vol 14 (9) ◽

pp. 6232-6243

Author(s):

J Zhou ◽

E N Olson

Keyword(s):

Transcriptional Activity ◽

Transcription Activation ◽

Bhlh Protein ◽

Specific Gene ◽

Phosphorylation Sites ◽

Gene Products ◽

Activation Domains ◽

Helix Loop Helix ◽

Carboxyl Terminal ◽

Bhlh Proteins

The muscle-specific basic helix-loop-helix (bHLH) protein myogenin activates muscle transcription by binding to target sequences in muscle-specific promoters and enhancers as a heterodimer with ubiquitous bHLH proteins, such as the E2A gene products E12 and E47. We show that dimerization with E2A products potentiates phosphorylation of myogenin at sites within its amino- and carboxyl-terminal transcription activation domains. Phosphorylation of myogenin at these sites was mediated by the bHLH region of E2A products and was dependent on dimerization but not on DNA binding. Mutations of the dimerization-dependent phosphorylation sites resulted in enhanced transcriptional activity of myogenin, suggesting that their phosphorylation diminishes myogenin's transcriptional activity. The ability of E2A products to potentiate myogenin phosphorylation suggests that dimerization induces a conformational change in myogenin that unmasks otherwise cryptic phosphorylation sites or that E2A proteins recruit a kinase for which myogenin is a substrate. That phosphorylation of these dimerization-dependent sites diminished myogenin's transcriptional activity suggests that these sites are targets for a kinase that interferes with muscle-specific gene expression.

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Suppression in Drosophila: su(Hw) and su(f) gene products interact with a region of gypsy (mdg4) regulating its transcriptional activity.

The EMBO Journal ◽

10.1002/j.1460-2075.1989.tb03451.x ◽

1989 ◽

Vol 8 (3) ◽

pp. 903-911 ◽

Cited By ~ 36

Author(s):

A. M. Mazo ◽

L. J. Mizrokhi ◽

A. A. Karavanov ◽

Y. A. Sedkov ◽

A. A. Krichevskaja ◽

...

Keyword(s):

Transcriptional Activity ◽

Gene Products ◽

F Gene

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Inactivation of the FLCN Tumor Suppressor Gene Induces TFE3 Transcriptional Activity by Increasing Its Nuclear Localization

PLoS ONE ◽

10.1371/journal.pone.0015793 ◽

2010 ◽

Vol 5 (12) ◽

pp. e15793 ◽

Cited By ~ 88

Author(s):

Seung-Beom Hong ◽

HyoungBin Oh ◽

Vladimir A. Valera ◽

Masaya Baba ◽

Laura S. Schmidt ◽

...

Keyword(s):

Tumor Suppressor ◽

Tumor Suppressor Gene ◽

Nuclear Localization ◽

Transcriptional Activity ◽

Suppressor Gene

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Transcriptional activity and constitutive nuclear localization of the ETS protein Elf-1

FEBS Letters ◽

10.1016/s0014-5793(97)00387-6 ◽

1997 ◽

Vol 408 (1) ◽

pp. 47-51 ◽

Cited By ~ 20

Author(s):

Isa Bredemeier-Ernst ◽

Alfred Nordheim ◽

Ralf Janknecht

Keyword(s):

Nuclear Localization ◽

Transcriptional Activity

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Sequence and functional analysis of the positively acting regulatory gene amdR from Aspergillus nidulans.

Molecular and Cellular Biology ◽

10.1128/mcb.10.6.3194 ◽

1990 ◽

Vol 10 (6) ◽

pp. 3194-3203 ◽

Cited By ~ 47

Author(s):

A Andrianopoulos ◽

M J Hynes

Keyword(s):

Dna Binding ◽

Aspergillus Nidulans ◽

Nuclear Localization ◽

Regulatory Gene ◽

Transcription Activation ◽

Binding Motif ◽

Wild Type ◽

Amino Terminal ◽

Carboxyl Terminal

The positively acting regulatory gene amdR of Aspergillus nidulans coordinately regulates the expression of five structural genes involved in the catabolism of certain amides (amdS), omega amino acids (gatA and gabA), and lactams (lamA and lamB) in the presence of omega amino acid inducers. Analysis of the amdR gene showed that it contains three small introns, heterogeneous 5' and 3' transcription sites, and multiple AUG codons prior to the major AUG initiator. The predicted amdR protein sequence has a cysteine-rich "zinc finger" DNA-binding motif at the amino-terminal end, four putative acidic transcription activation motifs in the carboxyl-terminal half, and two sequences homologous to the simian virus 40 large T antigen nuclear localization motif. These nuclear localization sequences overlap the cysteine-rich DNA-binding motif. A series of 5', 3', and internal deletions were examined in vivo for transcription activator function and showed that the amdR product contains at least two activation regions in the carboxyl-terminal half. Each of these activator amdR product contains at least two activation regions in the carboxyl-terminal half. Each of these activator regions may function independently, but both are required for wild-type levels of transcription activation. A number of the amdR deletion products were found to compete with the wild-type amdR product in vivo. Development of a rapid method for the localization of amdR mutations is presented, and using this technique, we localized and sequenced the mutation in the semiconstitutive amdR6c allele. The amdR6c missense mutation occurs in the middle of the gene, and it is suggested that it results in an altered protein which activates gene expression efficiently in the absence of an inducer.

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Isolation of a gene that down-regulates nitrate assimilation and influences another regulatory gene in the same system.

Molecular and Cellular Biology ◽

10.1128/mcb.9.9.4113 ◽

1989 ◽

Vol 9 (9) ◽

pp. 4113-4117 ◽

Cited By ~ 7

Author(s):

G J Sorger ◽

D Brown ◽

M Farzannejad ◽

A Guerra ◽

M Jonathan ◽

...

Keyword(s):

Neurospora Crassa ◽

Gene Product ◽

Regulatory Gene ◽

Nitrate Assimilation ◽

Gene Products ◽

Specific Pathway

Glutamine is the preferred source of nitrogen of Neurospora crassa. In its presence and that of the gene product of MS5 (nmr-1), the fungus represses the assimilation of less preferred forms of nitrogen, such as nitrate. In the absence of glutamine and the presence of the product of gene nit-2, less preferred forms of nitrogen are assimilated as long as a specific pathway for their assimilation is induced. We report here the isolation, from a cosmid bank, of a gene that complements MS5 and can also complement nit-2. We speculate that this result suggests an interaction between the MS5 and nit-2 gene products and that this is important in the regulation of nitrate assimilation.

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