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Characterizing the Interactomes of ABC Transporters PXA1 and PXA2 using the Integrated Split-Ubiquitin Membrane Yeast Two-hybrid SystemChuk, Matthew 13 January 2010 (has links)
The integrated Membrane Yeast Two-Hybrid technology (iMYTH) was employed to screen the ABCD family of ABC Transporters in S. cerevisiae. The two ABCD members, Pxa1p and Pxa2p were screened against yeast libraries which detected many interactors involved in expected biological processes in accordance with Pxa1p and Pxa2p’s annotated function (i.e. fatty acid metabolism), and unexpected new interactors that may elucidate a new role for the transporters (e.g. oxidative protection). Members of the glutaredoxins and thioredoxins, and associated proteins were found to interact with Pxa1p and Pxa2p. This may indicate that Pxa1p and Pxa2p also play a role in managing the redox environment, protecting against reactive oxygen species. The iMYTH technology was also used to show that Pxa2p is able to form homodimers, and that Pxa1p localization is directly or indirectly dependent on Pxa2p.
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Characterizing the Interactomes of ABC Transporters PXA1 and PXA2 using the Integrated Split-Ubiquitin Membrane Yeast Two-hybrid SystemChuk, Matthew 13 January 2010 (has links)
The integrated Membrane Yeast Two-Hybrid technology (iMYTH) was employed to screen the ABCD family of ABC Transporters in S. cerevisiae. The two ABCD members, Pxa1p and Pxa2p were screened against yeast libraries which detected many interactors involved in expected biological processes in accordance with Pxa1p and Pxa2p’s annotated function (i.e. fatty acid metabolism), and unexpected new interactors that may elucidate a new role for the transporters (e.g. oxidative protection). Members of the glutaredoxins and thioredoxins, and associated proteins were found to interact with Pxa1p and Pxa2p. This may indicate that Pxa1p and Pxa2p also play a role in managing the redox environment, protecting against reactive oxygen species. The iMYTH technology was also used to show that Pxa2p is able to form homodimers, and that Pxa1p localization is directly or indirectly dependent on Pxa2p.
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