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  1. Article ; Online: E. Peter Geiduschek.

    Geiduschek, E Peter

    Current biology : CB

    2010  Volume 20, Issue 17, Page(s) R694–5

    Abstract: Peter Geiduschek was an undergraduate Chemistry major at Columbia University and received ...

    Abstract Peter Geiduschek was an undergraduate Chemistry major at Columbia University and received his Physical Chemistry Ph.D. at Harvard in 1952 for research under the direction of Paul Doty. After short stints teaching chemistry at Yale and the University of Michigan, and an early two-year sabbatical asa US Army draftee, he came to the University of Chicago's Committee on Biophysics, where he was first introduced to enzymology and to phage. In 1970, he joined the Department of Biology of the then relatively new University of California campus at La Jolla, and has remained at UCSD since. His research contributions have primarily dealt with mechanisms of transcription and gene regulation, pursued in the specific microbial context of phage-infected bacteria, eukaryotes (budding yeast and RNA polymerase III) and archaea.
    MeSH term(s) Biology ; Chemistry, Physical ; Research ; United States
    Language English
    Publishing date 2010-05-15
    Publishing country England
    Document type Interview
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2010.06.067
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  2. Article ; Online: An introduction to transcription and gene regulation.

    Geiduschek, E Peter

    The Journal of biological chemistry

    2010  Volume 285, Issue 34, Page(s) 25885–25892

    MeSH term(s) Bacteriophages/genetics ; Biomedical Research/history ; Gene Expression Regulation, Viral ; History, 20th Century ; History, 21st Century ; Transcription, Genetic
    Language English
    Publishing date 2010-05-28
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.X110.143867
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  3. Article ; Online: Without a license, or accidents waiting to happen.

    Geiduschek, E Peter

    Annual review of biochemistry

    2009  Volume 78, Page(s) 1–28

    Abstract: This is a memoir of circumstances that have shaped my life as a scientist, some of the questions that have excited my interest, and some of the people with whom I have shared that pursuit. I was introduced to transcription soon after the discovery of RNA ...

    Abstract This is a memoir of circumstances that have shaped my life as a scientist, some of the questions that have excited my interest, and some of the people with whom I have shared that pursuit. I was introduced to transcription soon after the discovery of RNA polymerase and have been fascinated by questions relating to gene regulation since that time. My account touches on early experiments dealing with the ability of RNA polymerase to selectively transcribe its DNA template. Temporal programs of transcription that control the multiplication cycles of viruses (phages) and the precise mechanisms generating this regulation have been a continuing source of fascination and new challenges. A longtime interest in eukaryotic RNA polymerase III has centered on yeast and on the enumeration and properties of its transcription initiation factors, the architecture of its promoter complexes, and the mechanism of transcriptional initiation. These areas of research are widely regarded as separate, but to my thinking they have posed similar questions, and I have been unwilling or unable to abandon either one for the other. An additional interest in archaeal transcription can be seen as stemming naturally from this point of view.
    MeSH term(s) Austria ; Bacteriophages/genetics ; Bacteriophages/metabolism ; Biochemistry/history ; DNA-Directed RNA Polymerases ; History, 20th Century ; Transcription, Genetic ; United States ; Yeasts/genetics ; Yeasts/metabolism
    Chemical Substances DNA-Directed RNA Polymerases (EC 2.7.7.6)
    Language English
    Publishing date 2009
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portraits
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev.biochem.77.051906.142055
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  4. Article: An Introduction to Transcription and Gene Regulation

    Geiduschek, E. Peter

    Journal of biological chemistry. 2010 Aug. 20, v. 285, no. 34

    2010  

    Language English
    Dates of publication 2010-0820
    Size p. 25885-25892.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Transcription of the T4 late genes.

    Geiduschek, E Peter / Kassavetis, George A

    Virology journal

    2010  Volume 7, Page(s) 288

    Abstract: This article reviews the current state of understanding of the regulated transcription of the bacteriophage T4 late genes, with a focus on the underlying biochemical mechanisms, which turn out to be unique to the T4-related family of phages or ... ...

    Abstract This article reviews the current state of understanding of the regulated transcription of the bacteriophage T4 late genes, with a focus on the underlying biochemical mechanisms, which turn out to be unique to the T4-related family of phages or significantly different from other bacterial systems. The activator of T4 late transcription is the gene 45 protein (gp45), the sliding clamp of the T4 replisome. Gp45 becomes topologically linked to DNA through the action of its clamp-loader, but it is not site-specifically DNA-bound, as other transcriptional activators are. Gp45 facilitates RNA polymerase recruitment to late promoters by interacting with two phage-encoded polymerase subunits: gp33, the co-activator of T4 late transcription; and gp55, the T4 late promoter recognition protein. The emphasis of this account is on the sites and mechanisms of actions of these three proteins, and on their roles in the formation of transcription-ready open T4 late promoter complexes.
    MeSH term(s) Bacteriophage T4/genetics ; Bacteriophage T4/physiology ; DNA, Viral/metabolism ; Gene Expression Regulation, Viral ; Genes, Viral ; Promoter Regions, Genetic ; Protein Binding ; Transcription, Genetic ; Viral Proteins/metabolism
    Chemical Substances DNA, Viral ; Viral Proteins
    Language English
    Publishing date 2010-10-28
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 1743-422X
    ISSN (online) 1743-422X
    DOI 10.1186/1743-422X-7-288
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  6. Article ; Online: Dissection of the bacteriophage T4 late promoter complex.

    Nechaev, Sergei / Geiduschek, E Peter

    Journal of molecular biology

    2008  Volume 379, Issue 3, Page(s) 402–413

    Abstract: Activated transcription of the bacteriophage T4 late genes is generated by a mechanism that stands apart from the common modalities of transcriptional regulation: the activator is gp45, the viral replisome's sliding clamp; two sliding-clamp-binding ... ...

    Abstract Activated transcription of the bacteriophage T4 late genes is generated by a mechanism that stands apart from the common modalities of transcriptional regulation: the activator is gp45, the viral replisome's sliding clamp; two sliding-clamp-binding proteins, gp33 and gp55, replace the host RNA polymerase (RNAP) sigma subunit. We have mutagenized, reconfigured and selectively disrupted individual interactions of the sliding clamp with gp33 and gp55 and have monitored effects on transcription. The C-terminal sliding-clamp-binding epitopes of gp33 and gp55 are perfectly interchangeable, but the functions of these two RNAP-sliding clamp connections differ: only the gp33-gp45 linkage is essential for activation, while loss of the gp55-gp45 linkage impairs but does not abolish activation. Formation of transcription-ready promoter complexes by the sliding-clamp-activated wild-type T4 RNAP resists competition by high concentrations of the polyanion heparin. This avid formation of promoter complexes requires both linkages of the T4 late RNAP to the sliding clamp. Preopening the promoter compensates for loss of the gp55-gp45 but not the gp33-gp45 linkage. We interpret the relationship of these findings and our prior analysis to the common model of transcriptional initiation in bacteria in terms of two parallel pathways, with two RNAP holoenzymes and two DNA templates: (1) gp55-RNAP and the T4 late promoter execute basal transcription; (2) gp55-gp33-RNAP and the T4 late promoter with its mobile enhancer, the T4 sliding clamp, execute activated transcription. gp55 and gp33 perform sigma-like functions, gp55 in promoter recognition and gp33 (as well as gp55) in enhancer recognition. gp33 operates the switch between these two pathways by repressing basal transcription.
    MeSH term(s) Bacteriophage T4/genetics ; Bacteriophage T4/metabolism ; DNA Mutational Analysis ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Enzyme Activation ; Macromolecular Substances/metabolism ; Promoter Regions, Genetic ; Protein Conformation ; Transcription, Genetic ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Macromolecular Substances ; Viral Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; RNA polymerase alpha subunit (EC 2.7.7.6)
    Language English
    Publishing date 2008-04-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2008.03.071
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  7. Article: Transcription: adjusting to adversity by regulating RNA polymerase.

    Geiduschek, E Peter / Kassavetis, George A

    Current biology : CB

    2006  Volume 16, Issue 19, Page(s) R849–51

    Abstract: Under growth-limiting conditions, budding yeast shut down transcription of genes of the translation apparatus. Recent studies have shown that this response is signaled, in part, by multiple pathways that converge on Maf1, leading to a change of this ... ...

    Abstract Under growth-limiting conditions, budding yeast shut down transcription of genes of the translation apparatus. Recent studies have shown that this response is signaled, in part, by multiple pathways that converge on Maf1, leading to a change of this protein's phosphorylation state and its relocation to the nucleus, where it represses RNA polymerase III.
    MeSH term(s) Gene Expression Regulation ; Models, Genetic ; Phosphorylation ; RNA Polymerase III/genetics ; RNA Polymerase III/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription Factors/physiology ; Transcription, Genetic/physiology
    Chemical Substances MAF1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; RNA Polymerase III (EC 2.7.7.6)
    Language English
    Publishing date 2006-10-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2006.08.071
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  8. Article: The role of an upstream promoter interaction in initiation of bacterial transcription.

    Nechaev, Sergei / Geiduschek, E Peter

    The EMBO journal

    2006  Volume 25, Issue 8, Page(s) 1700–1709

    Abstract: The bacterial RNA polymerase (RNAP) recognizes promoters through sequence-specific contacts of its promoter-specificity components (sigma) with two DNA sequence motifs. Contacts with the upstream ('-35') promoter motif are made by sigma domain 4 attached ...

    Abstract The bacterial RNA polymerase (RNAP) recognizes promoters through sequence-specific contacts of its promoter-specificity components (sigma) with two DNA sequence motifs. Contacts with the upstream ('-35') promoter motif are made by sigma domain 4 attached to the flap domain of the RNAP beta subunit. Bacteriophage T4 late promoters consist solely of an extended downstream ('-10') motif specifically recognized by the T4 gene 55 protein (gp55). Low level basal transcription is sustained by gp55-RNAP holoenzyme. The late transcription coactivator gp33 binds to the beta flap and represses this basal transcription. Gp33 can also repress transcription by Escherichia coli sigma70-RNAP holoenzyme mutated to allow gp33 access to the beta flap. We propose that repression is due to gp33 blocking an upstream sequence-independent DNA-binding site on RNAP (as sigma70 domain 4 does) but, unlike sigma70 domain 4, providing no new DNA interaction. We show that this upstream interaction is essential only at an early step of transcription initiation, and discuss the role of this interaction in promoter recognition and transcriptional regulation.
    MeSH term(s) Bacterial Proteins/genetics ; Bacteriophage T4/genetics ; DNA, Bacterial/genetics ; DNA-Directed RNA Polymerases/genetics ; Escherichia coli/genetics ; Holoenzymes/genetics ; Holoenzymes/physiology ; Mutation ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Sigma Factor/genetics ; Transcription, Genetic ; Viral Proteins/genetics
    Chemical Substances Bacterial Proteins ; DNA, Bacterial ; Holoenzymes ; Sigma Factor ; Viral Proteins ; gene 33 protein, Enterobacteria phage T4 ; gene 55 protein, Enterobacteria phage T4 ; DNA-Directed RNA Polymerases (EC 2.7.7.6)
    Language English
    Publishing date 2006-04-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7601069
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  9. Article ; Online: Transcriptional activation in the context of repression mediated by archaeal histones.

    Wilkinson, Steven P / Ouhammouch, Mohamed / Geiduschek, E Peter

    Proceedings of the National Academy of Sciences of the United States of America

    2010  Volume 107, Issue 15, Page(s) 6777–6781

    Abstract: Many archaea (including all the methanogens, nearly all euryarchaeotes, and some crenarchaeotes) use histones as components of the chromatin that compacts their genomes. The archaeal histones are homo- and heterodimers that pair on DNA to form tetrasomes ...

    Abstract Many archaea (including all the methanogens, nearly all euryarchaeotes, and some crenarchaeotes) use histones as components of the chromatin that compacts their genomes. The archaeal histones are homo- and heterodimers that pair on DNA to form tetrasomes (as the eukaryotic histones H3 and H4 do). The resulting DNA packaging is known to interfere with assembly of the archaeal transcription apparatus at promoters; the ability of transcriptional activation to function in repressive archaeal chromatin has not yet been explored in vitro. Using four of the Methanocaldococcus jannaschii (Mja) histones, we have examined activation of the model Mja rb2 transcription unit by the Mja transcriptional activator Ptr2 in this simplified-chromatin context. Using hydroxyl radical footprinting, we find that the Ptr2-specific rb2 upstream activating site is a preferred histone-localizing site that nucleates histone: DNA-binding radiating from the rb2 promoter. Nevertheless, Ptr2 competes effectively with histones for access to the rb2 promoter and most potently activates transcription in vitro at histone concentrations that extensively coat DNA and essentially silence basal transcription.
    MeSH term(s) Archaea/genetics ; Archaea/metabolism ; Archaeal Proteins/metabolism ; Binding Sites ; Chromatin/chemistry ; DNA/chemistry ; DNA-Binding Proteins/metabolism ; Gene Silencing ; Genes, Archaeal ; Histones/chemistry ; Hydroxyl Radical ; Kinetics ; Models, Genetic ; Promoter Regions, Genetic ; Transcription, Genetic ; Transcriptional Activation
    Chemical Substances Archaeal Proteins ; Chromatin ; DNA-Binding Proteins ; Histones ; Ptr2 protein, Methanococcus jannaschii ; Hydroxyl Radical (3352-57-6) ; DNA (9007-49-2)
    Language English
    Publishing date 2010-03-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1002360107
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  10. Article: Archaeal transcription and its regulators.

    Geiduschek, E Peter / Ouhammouch, Mohamed

    Molecular microbiology

    2005  Volume 56, Issue 6, Page(s) 1397–1407

    Abstract: The relatively complex archaeal RNA polymerases are constructed along eukaryotic lines, and require two initiation factors for promoter recognition and specific transcription that are homologues of the RNA polymerase II TATA-binding protein and TFIIB. ... ...

    Abstract The relatively complex archaeal RNA polymerases are constructed along eukaryotic lines, and require two initiation factors for promoter recognition and specific transcription that are homologues of the RNA polymerase II TATA-binding protein and TFIIB. Many archaea also produce histones. In contrast, the transcriptional regulators encoded by archaeal genomes are primarily of bacterial rather than eukaryotic type. It is this combination of elements commonly regarded as separate and mutually exclusive that promises unifying insights into basic transcription mechanisms across all three domains of life.
    MeSH term(s) Archaea/genetics ; Archaea/metabolism ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Gene Expression Regulation, Archaeal ; Models, Molecular ; Transcription, Genetic
    Chemical Substances Archaeal Proteins
    Language English
    Publishing date 2005-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/j.1365-2958.2005.04627.x
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