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• W2084346383 abstract "Little is known about the interaction of pyrimidine nucleotides with G-proteins. Here we report that under experimental conditions that exclude transphosphorylation reactions, nucleoside 5′-triphosphates inhibited transducin-catalyzed GTP hydrolysis in the order of potency guanosine 5′-[γ-thio]triphosphate > GTP > guanosine 5′-[β,γ-imido]triphosphate > uridine 5′-[γ-thio]triphosphate > UTP > CTP. Nucleoside 5′-diphosphates inhibited GTP hydrolysis in the order of potency GDP ∼ guanosine 5′-[β-thio]thiodiphosphate > uridine 5′-[β-thio]diphosphate ⪢ UDP (no effect). UTP inhibited GTP hydrolysis competitively, indicative for nucleotide binding to the same site. Uracil nucleotides had a distinct activity profile with respect to disruption of the transitory complex between photoexcited rhodopsin and nucleotide-free transducin. We conclude that (i) uracil nucleotides bind to transducin-α with lower affinity than the corresponding guanine nucleotides, (ii) phosphorothioate modification of uracil nucleotides increases their affinity for transducin, and (iii) uracil nucleotides induce conformational changes in G-proteins that are different from the conformational changes induced by guanine nucleotides." @default.
• W2084346383 created "2016-06-24" @default.
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• W2084346383 date "1999-08-01" @default.
• W2084346383 modified "2023-09-25" @default.
• W2084346383 title "Interaction of the Retinal G-Protein Transducin with Uracil Nucleotides" @default.
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• W2084346383 doi "https://doi.org/10.1006/bbrc.1999.1203" @default.
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