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  • 1
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    The copyright issue (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):416.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841396" target="_blank"〉PubMed〈/a〉
    Keywords: *Authorship ; *Copyright ; Ownership ; *Periodicals as Topic ; Research Support as Topic
    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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    Enhancement of bacteriophage T4 late transcription by components of the T4 DNA replication apparatus (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-09-01
    Description: The expression of the late genes in bacteriophage T4 development is closely connected to viral DNA replication. Three T4-encoded DNA polymerase accessory proteins are shown to stimulate transcription at T4 late promoters in an adenosine triphosphate (ATP) hydrolysis-requiring process. The properties of the activation resemble those found for enhancers of eukaryotic transcription. However, the nature of the enhancer of T4 late transcription is novel in that it is a structure--a break in the nontranscribed DNA stand--to which the three replication proteins bind, rather than a sequence. Since the three DNA polymerase accessory proteins are carried on the moving replication fork as part of the replisome, we postulate that viral DNA replication forks act, in vivo, as the mobile enhancers of T4 late gene transcription. Whereas Escherichia coli RNA polymerase bearing the T4 gene 55 protein can selectively recognize T4 late promoters, it is only capable of responding to the transcription-enhancing activity of the three replication proteins on acquiring an additional T4-specific modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herendeen, D R -- Kassavetis, G A -- Barry, J -- Alberts, B M -- Geiduschek, E P -- New York, N.Y. -- Science. 1989 Sep 1;245(4921):952-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Center for Molecular Genetics, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2672335" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Replication ; DNA, Viral/*genetics ; DNA-Directed DNA Polymerase/metabolism ; DNA-Directed RNA Polymerases/metabolism ; *Enhancer Elements, Genetic ; Escherichia coli/*genetics ; Gene Expression Regulation ; *Genes, Viral ; Plasmids ; Promoter Regions, Genetic ; T-Phages/*genetics ; *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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  • 3
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    An RNA polymerase-binding protein that is required for communication between an enhancer and a promoter (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-04
    Description: Although bacteriophage T4 late promoters are selectively recognized by Escherichia coli RNA polymerase bearing a single protein encoded by T4 gene 55 (gp55), efficient transcription at these promoters requires enhancement by the three T4 DNA polymerase accessory proteins, bound to distal "mobile enhancer" sites. Two principles are shown to govern this transcriptional enhancement: (i) Promoter recognition and communication between the enhancer and the promoter require separate phage-coded proteins. Only RNA polymerase that has the T4 gene 33 protein (gp33) bound to it is subject to enhancement by the three DNA replication proteins. (ii) Transcriptional enhancement in this prokaryotic system is promoter-specific. Promoter specificity is generated by a direct competition of phage T4 gp33 and gp55 with the E. coli promoter recognition protein, sigma 70, for binding to the E. coli RNA polymerase core. Thus, polymerase that contains sigma 70 is competent to transcribe T4 early and middle genes, but lacks the ability to be enhanced by the DNA replication proteins, while polymerase that contains gp55 and gp33 is capable of enhancement via gp33, but its activity is restricted to T4 late promoters by gp55.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herendeen, D R -- Williams, K P -- Kassavetis, G A -- Geiduschek, E P -- New York, N.Y. -- Science. 1990 May 4;248(4955):573-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2185541" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/isolation & purification/*physiology ; DNA-Directed RNA Polymerases/*metabolism ; *Enhancer Elements, Genetic ; Escherichia coli/enzymology/*genetics ; Kinetics ; Models, Genetic ; *Promoter Regions, Genetic ; T-Phages/*genetics ; *Transcription Factors ; Viral Proteins/isolation & purification/*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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  • 4
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    A transcriptional enhancer whose function imposes a requirement that proteins track along DNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: Transcriptional regulation of the bacteriophage T4 late genes requires the participation of three DNA polymerase accessory proteins that are encoded by T4 genes 44, 62, and 45, and that act at an enhancer-like site. Transcriptional activation by these DNA replication proteins also requires the function of an RNA polymerase-bound coactivator protein that is encoded by T4 gene 33 and a promoter recognition protein that is encoded by T4 gene 55. Transcriptional activation in DNA constructs, in which the enhancer and a T4 late promoter can be segregated on two rings of a DNA catenane, has now been analyzed. The ability of an interposed DNA-binding protein to affect communication between the enhancer and the promoter was also examined. Together, these experiments demonstrate that this transcription-activating signal is conveyed between its enhancer and a T4 late promoter by a DNA-tracking mechanism. Alternative activation mechanisms relying entirely on through-space interactions of enhancer-bound and promoter-bound proteins are excluded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herendeen, D R -- Kassavetis, G A -- Geiduschek, E P -- New York, N.Y. -- Science. 1992 May 29;256(5061):1298-303.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0634.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598572" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA Replication ; DNA, Viral/*genetics/metabolism ; DNA-Directed DNA Polymerase/metabolism ; Deoxyribonuclease EcoRI/genetics/metabolism ; *Enhancer Elements, Genetic ; Escherichia coli/*genetics ; Gene Expression Regulation, Viral ; *Genes, Viral ; Models, Genetic ; Plasmids ; Restriction Mapping ; T-Phages/*genetics ; *Trans-Activators ; *Transcription, Genetic ; Transcriptional Activation ; Viral Proteins/genetics/*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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  • 5
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    Nucleosome mobility and the maintenance of nucleosome positioning (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-02
    Description: To study nucleosome mobility and positioning, the R3 lac repressor was used with an adenosine triphosphate (ATP)-dependent chromatin assembly system to establish the positioning of five nucleosomes, with one nucleosome located between two R3 lac operators. When R3 protein was dissociated from DNA with isopropyl beta-D-thiogalactopyranoside, the R3-induced nucleosome positions remained unchanged for at least 60 minutes in the absence of ATP but rearranged within 15 minutes in the presence of ATP. These results suggest that nucleosomes are dynamic and mobile rather than static and that a DNA binding factor is continuously required for the maintenance of nucleosome positioning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pazin, M J -- Bhargava, P -- Geiduschek, E P -- Kadonaga, J T -- New York, N.Y. -- Science. 1997 May 2;276(5313):809-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9115208" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Apyrase/metabolism ; Binding Sites ; Chromatin/*metabolism ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Isopropyl Thiogalactoside/pharmacology ; Nucleosomes/*physiology ; Operator Regions, Genetic ; Repressor Proteins/*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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  • 6
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    Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Nucleosomes, the nucleohistone subunits of chromatin, are present on transcribed eukaryotic genes but do not prevent transcription. It is shown here that the large yeast RNA polymerase III transcribes through a single nucleosome. This takes place through a direct internal nucleosome transfer in which histones never leave the DNA template. During this process, the polymerase pauses with a pronounced periodicity of 10 to 11 base pairs, which is consistent with restricted rotation in the DNA loop formed during transfer. Transcription through nucleosomes by the eukaryotic enzyme and by much smaller prokaryotic RNA polymerases thus shares many features, reflecting an important property of nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studitsky, V M -- Kassavetis, G A -- Geiduschek, E P -- Felsenfeld, G -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395401" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/chemistry/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Histones/metabolism ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleosomes/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase III/*metabolism ; Templates, Genetic ; *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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  • 7
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    Paths to activation of transcription (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1614-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0634, USA. epg@jeeves.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072826" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; *Bacterial Proteins ; Coliphages/genetics ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Enhancer Elements, Genetic ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Salmonella typhimurium/genetics ; Sigma Factor/metabolism ; *Trans-Activators ; Transcription Factors/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
    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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    Gifted public servants (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1996 May 17;272(5264):937-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638130" target="_blank"〉PubMed〈/a〉
    Keywords: *Administrative Personnel ; Government Agencies/*organization & administration ; National Institutes of Health (U.S.)/*organization & administration ; *Science ; United States
    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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    Gifted public servants (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1996 May 17;272(5264):937c-8c.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17745254" target="_blank"〉PubMed〈/a〉
    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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    RNA polymerase marching backward (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kassavetis, G A -- Geiduschek, E P -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):944-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California San Diego, La Jolla 92093-0634.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7679800" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Dna ; DNA Polymerase II/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology ; Humans ; Hydrolysis ; RNA/biosynthesis/*metabolism ; Templates, Genetic ; Transcription Factors/metabolism/pharmacology ; *Transcription Factors, TFII ; 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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