Oxidation mimicking substitution of conservative cysteine in recoverin suppresses its membrane association |
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Authors: | Permyakov Sergei E Zernii Evgeni Yu Knyazeva Ekaterina L Denesyuk Alexander I Nazipova Aliya A Kolpakova Tatiana V Zinchenko Dmitry V Philippov Pavel P Permyakov Eugene A Senin Ivan I |
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Institution: | 1.Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia ;2.Department of Biomedical Engineering, Pushchino State University, Pushchino, Moscow Region, 142290, Russia ;3.Department of Cell Signalling, A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, 119991, Russia ;4.Department of Biosciences, Åbo Akademi University, Turku, 20520, Finland ;5.Branch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia ; |
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Abstract: | Recoverin belongs to the family of intracellular Ca2+-binding proteins containing EF-hand domains, neuronal calcium sensors (NCS). In photoreceptor outer segments, recoverin is
involved into the recovery of visual cycle via Ca2+-dependent interaction with disk membranes and inhibition of rhodopsin kinase. The function of a conservative within NCS family
Cys residue in the inactive EF-loop 1 remains unclear, but previous study has shown its vulnerability to oxidation under mild
oxidizing conditions. To elucidate the influence of oxidation of the conservative Cys39 in recoverin the properties of its
C39D mutant, mimicking oxidative conversion of Cys39 into sulfenic, sulfinic or sulfonic acids have been studied using intrinsic
fluorescence, circular dichroism, and equilibrium centrifugation methods. The C39D substitution results in essential changes
in structural, physico-chemical and physiological properties of the protein: it reduces α-helical content, decreases thermal
stability and suppresses protein affinity for photoreceptor membranes. The latter effect precludes proper functioning of the
Ca2+-myristoyl switch in recoverin. The revealed significance of oxidation state of Cys39 for maintaining the protein functional
status shows that it may serve as redox sensor in vision and suggests an explanation of the available data on localization
and light-dependent translocation of recoverin in rod photoreceptors. |
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