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  • 1
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    Roles of phosphorylation sites in regulating activity of the transcription factor Pho4 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-13
    Description: Transcription factors are often phosphorylated at multiple sites. Here it is shown that multiple phosphorylation sites on the budding yeast transcription factor Pho4 play distinct and separable roles in regulating the factor's activity. Phosphorylation of Pho4 at two sites promotes the factor's nuclear export and phosphorylation at a third site inhibits its nuclear import. Phosphorylation of a fourth site blocks the interaction of Pho4 with the transcription factor Pho2. Multiple phosphorylation sites provide overlapping and partially redundant layers of regulation that function to efficiently control the activity of Pho4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Komeili, A -- O'Shea, E K -- New York, N.Y. -- Science. 1999 May 7;284(5416):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California-San Francisco, Department of Biochemistry and Biophysics, 513 Parnassus Avenue, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10320381" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/metabolism ; Amino Acid Substitution ; Cell Nucleus/*metabolism ; Cyclin-Dependent Kinases/metabolism ; Cyclins/metabolism ; *DNA-Binding Proteins ; Fungal Proteins/genetics/*metabolism ; *Homeodomain Proteins ; Karyopherins ; *Membrane Transport Proteins ; Nuclear Localization Signals ; Phosphorylation ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Trans-Activators/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Chromatin decouples promoter threshold from dynamic range (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-04-18
    Description: Chromatin influences gene expression by restricting access of DNA binding proteins to their cognate sites in the genome. Large-scale characterization of nucleosome positioning in Saccharomyces cerevisiae has revealed a stereotyped promoter organization in which a nucleosome-free region (NFR) is present within several hundred base pairs upstream of the translation start site. Many transcription factors bind within NFRs and nucleate chromatin remodelling events which then expose other cis-regulatory elements. However, it is not clear how transcription-factor binding and chromatin influence quantitative attributes of gene expression. Here we show that nucleosomes function largely to decouple the threshold of induction from dynamic range. With a series of variants of one promoter, we establish that the affinity of exposed binding sites is a primary determinant of the level of physiological stimulus necessary for substantial gene activation, and sites located within nucleosomal regions serve to scale expression once chromatin is remodelled. Furthermore, we find that the S. cerevisiae phosphate response (PHO) pathway exploits these promoter designs to tailor gene expression to different environmental phosphate levels. Our results suggest that the interplay of chromatin and binding-site affinity provides a mechanism for fine-tuning responses to the same cellular state. Moreover, these findings may be a starting point for more detailed models of eukaryotic transcriptional control.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435410/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435410/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lam, Felix H -- Steger, David J -- O'Shea, Erin K -- R01 GM051377/GM/NIGMS NIH HHS/ -- R01 GM051377-15/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2008 May 8;453(7192):246-50. doi: 10.1038/nature06867. Epub 2008 Apr 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Biology, Faculty of Arts and Sciences Center for Systems Biology, Harvard University, 7 Divinity Avenue, Bauer 307, Cambridge, Massachusetts 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18418379" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/*genetics/*metabolism ; DNA-Binding Proteins/genetics ; *Gene Expression Regulation, Fungal ; Genes, Fungal/genetics ; Genes, Reporter/genetics ; Models, Genetic ; Nucleosomes/genetics/metabolism ; Peptide Chain Initiation, Translational ; Phosphates/pharmacology ; Promoter Regions, Genetic/*genetics ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins/genetics ; Transcription Factors/genetics ; Transcriptional Activation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Preferential heterodimer formation by isolated leucine zippers from fos and jun (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-08-11
    Description: The products of the nuclear oncogenes fos and jun are known to form heterodimers that bind to DNA and modulate transcription. Both proteins contain a leucine zipper that is important for heterodimer formation. Peptides corresponding to these leucine zippers were synthesized. When mixed, these peptides preferentially form heterodimers over homodimers by at least 1000-fold. Both homodimers and the heterodimer are parallel alpha helices. The leucine zipper regions from Fos and Jun therefore correspond to autonomous helical dimerization sites that are likely to be short coiled coils, and these regions are sufficient to determine the specificity of interaction between Fos and Jun. The Fos leucine zipper forms a relatively unstable homodimer. Instability of homodimers provides a thermodynamic driving force for preferential heterodimer formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, E K -- Rutkowski, R -- Stafford, W F 3rd -- Kim, P S -- RR05711/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1989 Aug 11;245(4918):646-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2503872" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Circular Dichroism ; *DNA-Binding Proteins ; Disulfides ; *Leucine ; Macromolecular Substances ; Molecular Sequence Data ; Peptide Fragments/chemical synthesis ; Protein Conformation ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-fos ; Proto-Oncogene Proteins c-jun ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-07
    Description: A genetic system was developed in Escherichia coli to study leucine zippers with the amino-terminal domain of bacteriophage lambda repressor as a reporter for dimerization. This system was used to analyze the importance of the amino acid side chains at eight positions that form the hydrophobic interface of the leucine zipper dimer from the yeast transcriptional activator, GCN4. When single amino acid substitutions were analyzed, most functional variants contained hydrophobic residues at the dimer interface, while most nonfunctional sequence variants contained strongly polar or helix-breaking residues. In multiple randomization experiments, however, many combinations of hydrophobic residues were found to be nonfunctional, and leucines in the heptad repeat were shown to have a special function in leucine zipper dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, J C -- O'Shea, E K -- Kim, P S -- Sauer, R T -- AI15706/AI/NIAID NIH HHS/ -- GM11117/GM/NIGMS NIH HHS/ -- GM44162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2147779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage lambda/*genetics ; DNA-Binding Proteins/*genetics ; Escherichia coli/*genetics ; Fungal Proteins/*genetics ; Genetic Variation ; Leucine Zippers/*genetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phenotype ; Protein Conformation ; *Protein Kinases ; Random Allocation ; Recombinant Fusion Proteins/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Evidence that the leucine zipper is a coiled coil (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-27
    Description: Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues. A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized. This peptide associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation. Although some features of the leucine zipper model are supported by our experimental data, the peptide has the characteristics of a coiled coil.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, E K -- Rutkowski, R -- Kim, P S -- New York, N.Y. -- Science. 1989 Jan 27;243(4890):538-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911757" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromatography, High Pressure Liquid ; Circular Dichroism ; DNA/metabolism ; *DNA-Binding Proteins ; Disulfides ; *Fungal Proteins ; *Leucine ; Macromolecular Substances ; Molecular Sequence Data ; Peptide Fragments ; Protein Conformation ; *Protein Kinases ; Repetitive Sequences, Nucleic Acid ; *Saccharomyces cerevisiae Proteins ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, E K -- Klemm, J D -- Kim, P S -- Alber, T -- GM 44162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948029" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Computer Simulation ; DNA-Binding Proteins/*chemistry ; Fungal Proteins/*chemistry ; Hydrogen Bonding ; *Leucine Zippers ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Protein Kinases ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*chemistry ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Ordered phosphorylation governs oscillation of a three-protein circadian clock (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-10-06
    Description: The simple circadian oscillator found in cyanobacteria can be reconstituted in vitro using three proteins-KaiA, KaiB, and KaiC. The total phosphorylation level of KaiC oscillates with a circadian period, but the mechanism underlying its sustained oscillation remains unclear. We have shown that four forms of KaiC differing in their phosphorylation state appear in an ordered pattern arising from the intrinsic autokinase and autophosphatase rates of KaiC and their modulation by KaiA. Kinetic and biochemical data indicate that one of these phosphoforms inhibits the activity of KaiA through interaction with KaiB, providing the crucial feedback that sustains oscillation. A mathematical model constrained by experimental data quantitatively reproduces the circadian period and the distinctive dynamics of the four phosphoforms.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2427396/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2427396/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rust, Michael J -- Markson, Joseph S -- Lane, William S -- Fisher, Daniel S -- O'Shea, Erin K -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):809-12. Epub 2007 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Faculty of Arts and Sciences Center for Systems Biology, Departments of Molecular and Cellular Biology and of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916691" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*physiology ; Biological Clocks/*physiology ; Circadian Rhythm/*physiology ; Circadian Rhythm Signaling Peptides and Proteins ; Models, Biological ; Phosphorylation ; Synechococcus/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Tunable signal processing through modular control of transcription factor translocation (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-01-26
    Description: Signaling pathways can induce different dynamics of transcription factor (TF) activation. We explored how TFs process signaling inputs to generate diverse dynamic responses. The budding yeast general stress-responsive TF Msn2 acted as a tunable signal processor that could track, filter, or integrate signals in an input-dependent manner. This tunable signal processing appears to originate from dual regulation of both nuclear import and export by phosphorylation, as mutants with one form of regulation sustained only one signal-processing function. Versatile signal processing by Msn2 is crucial for generating distinct dynamic responses to different natural stresses. Our findings reveal how complex signal-processing functions are integrated into a single molecule and provide a guide for the design of TFs with "programmable" signal-processing functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746486/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746486/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hao, Nan -- Budnik, Bogdan A -- Gunawardena, Jeremy -- O'Shea, Erin K -- R01 GM081578/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 Jan 25;339(6118):460-4. doi: 10.1126/science.1227299.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard University Faculty of Arts and Sciences Center for Systems Biology, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23349292" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Cell Nucleus/*metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/genetics/metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/*metabolism ; Models, Biological ; Nuclear Export Signals ; Nuclear Localization Signals ; Osmotic Pressure ; Oxidative Stress ; Phosphorylation ; Proteins/pharmacology ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*metabolism ; *Signal Transduction ; Stress, Physiological ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Robust circadian oscillations in growing cyanobacteria require transcriptional feedback (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-05-11
    Description: The remarkably stable circadian oscillations of single cyanobacteria enable a population of growing cells to maintain synchrony for weeks. The cyanobacterial pacemaker is a posttranslational regulation (PTR) circuit that generates circadian oscillations in the phosphorylation state of the clock protein KaiC. Layered on top of the PTR is transcriptional-translational feedback regulation (TTR), common to all circadian systems, consisting of a negative feedback loop in which KaiC regulates its own production. We found that the PTR circuit is sufficient to generate oscillations in growing cyanobacteria. However, in the absence of TTR, individual oscillators were less stable and synchrony was not maintained in a population of cells. Experimentally constrained mathematical modeling reproduced sustained oscillations in the PTR circuit alone and demonstrated the importance of TTR for oscillator synchrony.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3696982/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3696982/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teng, Shu-Wen -- Mukherji, Shankar -- Moffitt, Jeffrey R -- de Buyl, Sophie -- O'Shea, Erin K -- 1R21AI094363-01A1/AI/NIAID NIH HHS/ -- R21 AI094363/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 May 10;340(6133):737-40. doi: 10.1126/science.1230996.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Faculty of Arts and Sciences Center for Systems Biology, Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23661759" target="_blank"〉PubMed〈/a〉
    Keywords: Circadian Rhythm/*genetics ; *Feedback, Physiological ; Protein Biosynthesis ; Synechococcus/genetics/*physiology ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Regulation of chromatin remodeling by inositol polyphosphates (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: Chromatin remodeling is required for efficient transcription of eukaryotic genes. In a genetic selection for budding yeast mutants that were defective in induction of the phosphate-responsive PHO5 gene, we identified mutations in ARG82/IPK2, which encodes a nuclear inositol polyphosphate kinase. In arg82 mutant strains, remodeling of PHO5 promoter chromatin is impaired, and the adenosine triphosphate-dependent chromatin-remodeling complexes SWI/SNF and INO80 are not efficiently recruited to phosphate-responsive promoters. These results suggest a role for the small molecule inositol polyphosphate in the regulation of chromatin remodeling and transcription.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458531/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458531/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steger, David J -- Haswell, Elizabeth S -- Miller, Aimee L -- Wente, Susan R -- O'Shea, Erin K -- GM51219/GM/NIGMS NIH HHS/ -- GM51377/GM/NIGMS NIH HHS/ -- R01 GM051377/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 3;299(5603):114-6. Epub 2002 Nov 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434012" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Chromatin/*metabolism ; DNA-Binding Proteins/metabolism ; Fungal Proteins/genetics/metabolism ; Gene Expression Regulation, Fungal ; Inositol Phosphates/*metabolism ; Mutation ; *Nuclear Proteins ; Phosphate Transport Proteins/*genetics/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/genetics/metabolism ; Point Mutation ; Promoter Regions, Genetic ; Protein Binding ; Proton-Phosphate Symporters/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Saccharomycetales/genetics/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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