Person: Boeszoermenyi, Andras
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Boeszoermenyi
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Andras
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Boeszoermenyi, Andras
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Publication Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment(Nature Publishing Group UK, 2018) Robson, Scott; Takeuchi, Koh; Boeszoermenyi, Andras; Coote, Paul; Dubey, Abhinav; Hyberts, Sven; Wagner, Gerhard; Arthanari, HaribabuBackbone resonance assignment is a critical first step in the investigation of proteins by NMR. This is traditionally achieved with a standard set of experiments, most of which are not optimal for large proteins. Of these, HNCA is the most sensitive experiment that provides sequential correlations. However, this experiment suffers from chemical shift degeneracy problems during the assignment procedure. We present a strategy that increases the effective resolution of HNCA and enables near-complete resonance assignment using this single HNCA experiment. We utilize a combination of 2-13C and 3-13C pyruvate as the carbon source for isotope labeling, which suppresses the one bond (1Jαβ) coupling providing enhanced resolution for the Cα resonance and amino acid-specific peak shapes that arise from the residual coupling. Using this approach, we can obtain near-complete (>85%) backbone resonance assignment of a 42 kDa protein using a single HNCA experiment.Publication Inhibiting Fungal Multidrug Resistance by Disrupting an Activator-Mediator Interaction(2016) Nishikawa, Joy; Boeszoermenyi, Andras; Vale-Silva, Luis A.; Torelli, Riccardo; Posteraro, Brunella; Sohn, Yoo-Jin; Ji, Fei; Gelev, Vladimir; Sanglard, Dominique; Sanguinetti, Maurizio; Sadreyev, Ruslan; Mukherjee, Goutam; Bhyravabhotla, Jayaram; Buhrlage, Sara; Gray, Nathanael; Wagner, Gerhard; Naar, Anders; Arthanari, HaribabuPublication Structural basis for LeishIF4E-1 modulation by an interacting protein in the human parasite Leishmania major(Oxford University Press, 2018) Meleppattu, Shimi; Arthanari, Haribabu; Zinoviev, Alexandra; Boeszoermenyi, Andras; Wagner, Gerhard; Shapira, Michal; Leger-Abraham, MelissaAbstract Leishmania parasites are unicellular pathogens that are transmitted to humans through the bite of infected sandflies. Most of the regulation of their gene expression occurs post-transcriptionally, and the different patterns of gene expression required throughout the parasites’ life cycle are regulated at the level of translation. Here, we report the X-ray crystal structure of the Leishmania cap-binding isoform 1, LeishIF4E-1, bound to a protein fragment of previously unknown function, Leish4E-IP1, that binds tightly to LeishIF4E-1. The molecular structure, coupled to NMR spectroscopy experiments and in vitro cap-binding assays, reveal that Leish4E-IP1 allosterically destabilizes the binding of LeishIF4E-1 to the 5′ mRNA cap. We propose mechanisms through which Leish4E-IP1-mediated LeishIF4E-1 inhibition could regulate translation initiation in the human parasite.