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An investigation into the control of genetic recombination in some strains of Neurospora crassaGriffiths, Anthony John Frederick 10 1900 (has links)
The understanding of basic cellular processes has been greatly facilitated through investigation of the behaviour of mutant forms. In a similar way the mechanisms of genetic recombination may be clarified by a study of strains which are known to show inherited differences in recombination behaviour at meiosis. The haploid fungus Neurospora crassa is particularly well suited to such an investigation since recombination frequency heterogeneity has been extensively reported in that organism, and the differences are believed to be, to a large extent, under genetic control. Strains showing recombination frequency heterogeneity over a marked genetic region have been extensively analysed in the present work and the mode of action of the factors controlling recombination frequency has been investigated by combining differing strains in heterokaryons. / Thesis / Doctor of Philosophy (PhD)
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Protein Profiles of <i>Neurospora Crassa</i> and the Effects of <i>NIT-2</i> Under Varying Levels of Nitrogen AvailabilityWerry, Michael P. 18 September 2013 (has links)
No description available.
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Studies on Quinic Acid (QA) Gene Cluster in Various Strains of Neurospora CrassaVeeramachaneni, Rathna J. 14 October 2010 (has links)
No description available.
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Expression kinetics of the quinic acid (qa) gene cluster in Neurospora crassaFleeger, Melissa 07 March 2011 (has links)
No description available.
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Protein Profiling of Wild-type <i>Neurospora crassa</i> Grown on Various Carbon SourcesAllen, Katie 09 March 2011 (has links)
No description available.
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Induction of the qa-y and qa-1F Genes in Neurospora crassa at Differing Times of Quinic Acid ExposureGeorge, Kory 03 June 2016 (has links)
No description available.
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Changes in Gene Expression of Neurospora crassa in Response to Quinic AcidBrown, Kayla A. January 2016 (has links)
No description available.
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Isolation and characterization of pco-1, which encodes a regulatory protein that controls purine degradation in neurospora crassaLiu, Ta-Wei David January 2003 (has links)
No description available.
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Études Structurales par Résonance Magnétique Nucléaire (RMN) du Site Actif du Ribozyme VS de Neurospora.Desjardins-Séguin, Geneviève 11 1900 (has links)
Nous étudions le ribozyme VS de Neurospora, en tant que système modèle, pour
augmenter nos connaissances sur la relation entre la structure et la fonction chez les ARNs,
ainsi que pour mieux comprendre le mécanisme de clivage de ce ribozyme. Il a été proposé
précédemment que la boucle interne A730 dans la tige-boucle VI (SLVI) contient le site actif
du ribozyme et lie un ou plusieurs ions métalliques qui pourraient participer au mécanisme
réactionnel. Nous avons déterminé par spectroscopie RMN la structure de la tige-boucle SLVI
contenant la boucle A730 afin d’éclaircir ce mécanisme. La structure obtenue est en accord
avec les études biochimiques antérieures et présente un ou plusieurs sites de liaison au
magnésium associé à la boucle interne. Suite à des études de cinétique et de mutagenèse, il
a été proposé qu’une adénine localisée dans le site actif, A756, participe à la catalyse par
acide/base générale. Des études de pH effectuées précédemment ont identifié un pKa
catalytique (5.2-5.8) qui correspond probablement à l’équilibre de protonation du A756. À
l’aide de méthodes utilisant le carbone-13, nous avons identifié un pKa modifié appartenant au
A756, ce qui supporte le rôle de ce résidu dans la catalyse par acide/base générale. Les
études structurales présentées ici aident donc à augmenter notre compréhension du
mécanisme de clivage chez le ribozyme VS. / We are studying the Neurospora VS ribozyme as a model system to increase our
knowledge of the structure-function relationship in RNA and to better understand the
mechanism of the cleavage reaction. It has been previously postulated that the A730 internal
loop of stem-loop VI (SLVI) forms the active site of the VS ribozyme and binds magnesium
ion(s) that may participate in catalysis. To get insights into the catalytic mechanism, we have
determined by NMR spectroscopy the structure of a SLVI fragment containing the A730 loop.
The structure we obtained is in agreement with previous biochemical studies and contains one
or more magnesium-ion binding sites in the active site. Based on kinetic and mutagenesis
studies, it has been proposed that an adenine in the A730 loop, A756, is important for catalysis
and may participate in general acid/base catalysis. Previous pH-dependent enzymatic studies
identified a catalytic pKa of 5.2-5.8, which likely corresponds to the protonation equilibrium of
this A756 adenine in the A730 loop. Using 13C NMR methods, we have identified a shifted pKa
for A756, which gives additional support to the role of this residue in the general acid/base
mechanism. The NMR studies presented here therefore increase our understanding of the
cleavage reaction in the VS ribozyme.
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Études Structurales par Résonance Magnétique Nucléaire (RMN) du Site Actif du Ribozyme VS de NeurosporaDesjardins-Séguin, Geneviève 11 1900 (has links)
No description available.
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