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The decrement in light sensitivity of the isolated frog retinal rod in the presence of a phosphorylation-resistant GDP analogue of guanosine-5′-O-(2-thiodiphosphate) as a confirmation of the hypothesis about transducin activation via the transphosphorylation mechanism

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Abstract

The decrement in light sensitivity of the isolated frog retinal rod cell was demonstrated after a short-time perfusion with guanosine-5′-O-(2-thiodiphosphate), which is an analog of GDP that is resistant to phosphorylation by nucleoside diphosphate kinase. This decrement can be explained by the hypothesis that transducin, which is the main GTP-binding protein of the retinal rod photoreceptor of vertebrates, is activated by phosphorylation of bound GDP to GTP; this is induced by the activated rhodopsin receptor. The results can be considered as a confirmation of the proposed hypothesis.

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Abbreviations

G proteins:

heterotrimeric GTP-binding proteins

R*:

photoactivated rhodopsin

NDP kinase:

nucleoside diphosphate kinase

GDP[S]:

guanosine-5’-O-(2-thiodiphosphate)

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Authors and Affiliations

  1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, ul. Institutskaya 3, Pushchino, Moscow oblast, 142290, Russia

    O. V. Petrukhin, T. G. Orlova, A. R. Nezvetsky & N. Ya. Orlov

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  1. O. V. Petrukhin
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  2. T. G. Orlova
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  3. A. R. Nezvetsky
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  4. N. Ya. Orlov
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Correspondence to O. V. Petrukhin.

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Original Russian Text © O.V. Petrukhin, T.G. Orlova, A.R. Nezvetsky, N.Ya. Orlov, 2016, published in Biofizika, 2016, Vol. 61, No. 5, pp. 879–883.

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Petrukhin, O.V., Orlova, T.G., Nezvetsky, A.R. et al. The decrement in light sensitivity of the isolated frog retinal rod in the presence of a phosphorylation-resistant GDP analogue of guanosine-5′-O-(2-thiodiphosphate) as a confirmation of the hypothesis about transducin activation via the transphosphorylation mechanism. BIOPHYSICS 61, 884–887 (2016). https://doi.org/10.1134/S0006350916050249

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