Search Results - (Author, Cooperation:M. Quail)

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  1. 1
    K. Howe ; M. D. Clark ; C. F. Torroja ; J. Torrance ; C. Berthelot ; M. Muffato ; J. E. Collins ; S. Humphray ; K. McLaren ; L. Matthews ; S. McLaren ; I. Sealy ; M. Caccamo ; C. Churcher ; C. Scott ; J. C. Barrett ; R. Koch ; G. J. Rauch ; S. White ; W. Chow ; B. Kilian ; L. T. Quintais ; J. A. Guerra-Assuncao ; Y. Zhou ; Y. Gu ; J. Yen ; J. H. Vogel ; T. Eyre ; S. Redmond ; R. Banerjee ; J. Chi ; B. Fu ; E. Langley ; S. F. Maguire ; G. K. Laird ; D. Lloyd ; E. Kenyon ; S. Donaldson ; H. Sehra ; J. Almeida-King ; J. Loveland ; S. Trevanion ; M. Jones ; M. Quail ; D. Willey ; A. Hunt ; J. Burton ; S. Sims ; K. McLay ; B. Plumb ; J. Davis ; C. Clee ; K. Oliver ; R. Clark ; C. Riddle ; D. Elliot ; G. Threadgold ; G. Harden ; D. Ware ; S. Begum ; B. Mortimore ; G. Kerry ; P. Heath ; B. Phillimore ; A. Tracey ; N. Corby ; M. Dunn ; C. Johnson ; J. Wood ; S. Clark ; S. Pelan ; G. Griffiths ; M. Smith ; R. Glithero ; P. Howden ; N. Barker ; C. Lloyd ; C. Stevens ; J. Harley ; K. Holt ; G. Panagiotidis ; J. Lovell ; H. Beasley ; C. Henderson ; D. Gordon ; K. Auger ; D. Wright ; J. Collins ; C. Raisen ; L. Dyer ; K. Leung ; L. Robertson ; K. Ambridge ; D. Leongamornlert ; S. McGuire ; R. Gilderthorp ; C. Griffiths ; D. Manthravadi ; S. Nichol ; G. Barker ; S. Whitehead ; M. Kay ; J. Brown ; C. Murnane ; E. Gray ; M. Humphries ; N. Sycamore ; D. Barker ; D. Saunders ; J. Wallis ; A. Babbage ; S. Hammond ; M. Mashreghi-Mohammadi ; L. Barr ; S. Martin ; P. Wray ; A. Ellington ; N. Matthews ; M. Ellwood ; R. Woodmansey ; G. Clark ; J. Cooper ; A. Tromans ; D. Grafham ; C. Skuce ; R. Pandian ; R. Andrews ; E. Harrison ; A. Kimberley ; J. Garnett ; N. Fosker ; R. Hall ; P. Garner ; D. Kelly ; C. Bird ; S. Palmer ; I. Gehring ; A. Berger ; C. M. Dooley ; Z. Ersan-Urun ; C. Eser ; H. Geiger ; M. Geisler ; L. Karotki ; A. Kirn ; J. Konantz ; M. Konantz ; M. Oberlander ; S. Rudolph-Geiger ; M. Teucke ; C. Lanz ; G. Raddatz ; K. Osoegawa ; B. Zhu ; A. Rapp ; S. Widaa ; C. Langford ; F. Yang ; S. C. Schuster ; N. P. Carter ; J. Harrow ; Z. Ning ; J. Herrero ; S. M. Searle ; A. Enright ; R. Geisler ; R. H. Plasterk ; C. Lee ; M. Westerfield ; P. J. de Jong ; L. I. Zon ; J. H. Postlethwait ; C. Nusslein-Volhard ; T. J. Hubbard ; H. Roest Crollius ; J. Rogers ; D. L. Stemple
    Nature Publishing Group (NPG)
    Published 2013
    Staff View
    Publication Date:
    2013-04-19
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Chromosomes/genetics ; Conserved Sequence/*genetics ; Evolution, Molecular ; Female ; Genes/genetics ; Genome/*genetics ; Genome, Human/genetics ; Genomics ; Humans ; Male ; Meiosis/genetics ; Molecular Sequence Annotation ; Pseudogenes/genetics ; Reference Standards ; Sex Determination Processes/genetics ; Zebrafish/*genetics ; Zebrafish Proteins/genetics
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Quail, M. A. ; Haydon, D. J. ; Guest, J. R.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1994
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    Transcript mapping and studies with lacZ translational fusions have shown that the pdhR gene (formerly genA) is the proximal gene of the pdhR–aceE–aceF–Ipd operon encoding the pyruvate dehydrogenase (PDH) complex of Escherichia coli. A pdhR–lpd read-through transcript (7.4 kb) initiating at the pyruvate-inducible pdh promoter, and a smaller lpd transcript (1.7 kb) initiating at the independent lpd promoter, were identified. Evidence showing that the pdhR gene product negatively regulates the synthesis of the PdhR protein and the PDH complex via the pdh promoter was obtained, with pyruvate (or a derivative) serving as the putative inducing coeffector. The partially purified PdhR protein was also found to specifically retard and protect DNA fragments containing the pdh promoter region. The pdh promoter was not strongly controlled by ArcA, FNR or CRP.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  3. 3
    Quail, M. A. ; Guest, J. R.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1995
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The repressor of the pdhR–aceEF–lpd operon of Escherichia coli, PdhR, was amplified to 23% of total cell protein and purified to homogeneity by heparin–agarose and catlon-exchange chromatography. The purified protein is a monomer (Mr 29300) which binds specifically to DNA fragments containing the pdh promoter (Ppdh) in the absence of pyruvate. The pdh operator was identified by DNase I footprinting as a region of hyphenated dyad symmetry, +11AATTGGTaagACCAATT+27, situated just downstream of the transcript start site. In vitro transcription from Ppdh was repressed 〉 1000-fold by PdhR and this repression was antagonized in a concentration-dependent manner by its co-effector, pyruvate. Studies on RNA polymerase binding at Ppdh showed that RNA polymerase protects the -44 to +21 region in the absence of PdhR, but no RNA polymerase binding or protection upstream of +9 could be detected in the presence of PdhR. It is concluded that PdhR represses transcription by binding to an operator site centred at +19 such that effective binding of RNA polymerase is prevented.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  4. 4
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The sequencing of the entire genetic complement of Streptomyces coelicolor A3(2) has been completed with the determination of the 365 023 bp sequence of the linear plasmid SCP1. Remarkably, the functional distribution of SCP1 genes somewhat resembles that of the chromosome: predicted gene products/functions include ECF sigma factors, antibiotic biosynthesis, a gamma-butyrolactone signalling system, members of the actinomycete-specific Wbl class of regulatory proteins and 14 secreted proteins. Some of these genes are among the 18 that contain a TTA codon, making them targets for the developmentally important tRNA encoded by the bldA gene. RNA analysis and gene fusions showed that one of the TTA-containing genes is part of a large bldA-dependent operon, the gene products of which include three proteins isolated from the spore surface by detergent washing (SapC, D and E), and several probable metabolic enzymes. SCP1 shows much evidence of recombinational interactions with other replicons and transposable elements during its history. For example, it has two sets of partitioning genes (which may explain why an integrated copy of SCP1 partially suppressed the defective partitioning of a parAB-deleted chromosome during sporulation). SCP1 carries a cluster of probable transfer determinants and genes encoding likely DNA polymerase III subunits, but it lacks an obvious candidate gene for the terminal protein associated with its ends. This may be related to atypical features of its end sequences.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  5. 5
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] Campylobacter jejuni, from the delta-epsilon group of proteobacteria, is a microaerophilic, Gram-negative, flagellate, spiral bacterium—properties it shares with the related gastric pathogen Helicobacter pylori. It is the leading cause of bacterial food-borne diarrhoeal disease ...
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  6. 6
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] Analysis of Plasmodium falciparum chromosome 3, and comparison with chromosome 2, highlights novel features of chromosome organization and gene structure. The sub-telomeric regions of chromosome 3 show a conserved order of features, including repetitive DNA sequences, members of multigene families ...
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  7. 7
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] Streptomyces coelicolor is a representative of the group of soil-dwelling, filamentous bacteria responsible for producing most natural antibiotics used in human and veterinary medicine. Here we report the 8,667,507 base pair linear chromosome of this organism, containing the largest number of genes ...
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  8. 8
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] Neisseria meningitidis causes bacterial meningitis and is therefore responsible for considerable morbidity and mortality in both the developed and the developing world. Meningococci are opportunistic pathogens that colonize the nasopharynges and oropharynges of asymptomatic carriers. For ...
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses
  9. 9
    Staff View
    ISSN:
    1432-1327
    Keywords:
    Key words Dinuclear centre ; Diiron site ; Ferritin ; Iron oxidation ; Bacterial ferritin
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Chemistry and Pharmacology
    Notes:
    Abstract  The ferritin of Escherichia coli (EcFtnA) is similar to human H-chain ferritin (HuHF) in having 24 subunits, each containing a dinuclear site at which two iron atoms can be oxidised (the diiron centre). In EcFtnA, unlike HuHF, fluorescence quenching of Trp122, located near site A of the dinuclear centre, can be used to monitor metal binding (this tryptophan is absent from HuHF). Metal binding also perturbs the UV absorbance spectrum of Trp122 and that of Tyr24 (a conserved residue near site B of the dinuclear centre). Using UV-difference spectroscopy and fluorescence quenching it is shown that Fe(II) and Zn(II) bind at the same sites, A and B. Sequential stopped-flow studies of Fe(II) binding and oxidation also show that Zn(II) is an effective competitor of Fe(II) binding and an inhibitor of its oxidation.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses