Elements of the C-terminal tail of a C-terminal domain homolog of the Orange Carotenoid Protein determining xanthophyll uptake from liposomes

Likkei, K.; Moldenhauer, M.; Tavraz, N.N.; Egorkin, N.A.; Slonimskiy, Y.B.; Maksimov, E.G.; Sluchanko, N.N.; Friedrich, T.

Авторы: Likkei Kristina, Moldenhauer Marcus, Tavraz Neslihan N., Egorkin Nikita A., Slonimskiy Yury B., Maksimov Eugene G., Sluchanko Nikolai N., Friedrich Thomas
Журнал: Biochimica et Biophysica Acta - Bioenergetics
Том: 1865
Номер: 3
Год издания: 2024
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Номер статьи: 149043
DOI: 10.1016/j.bbabio.2024.149043
Аннотация: arotenoids perform multifaceted roles in life ranging from coloration over light harvesting to photoprotection. The Orange Carotenoid Protein (OCP), a light-driven photoswitch involved in cyanobacterial photoprotection, accommodates a ketocarotenoid vital for its function. OCP extracts its ketocarotenoid directly from membranes, or accepts it from homologs of its C-terminal domain (CTDH). The CTDH from Anabaena (AnaCTDH) was shown to be important for carotenoid transfer and delivery from/to membranes. The C-terminal tail of AnaCTDH is a critical structural element likely serving as a gatekeeper and facilitator of carotenoid uptake from membranes. We investigated the impact of amino acid substitutions within the AnaCTDH-CTT on echinenone and canthaxanthin uptake from DOPC and DMPG liposomes. The transfer rate was uniformly reduced for substitutions of Arg-137 and Arg-138 to Gln or Ala, and depended on the lipid type, indicating a weaker interaction particularly with the lipid head group. Our results further suggest that Glu-132 has a membrane-anchoring effect on the PC lipids, specifically at the choline motif as inferred from the strongly different effects of the CTT variants on the extraction from the two liposome types. The substitution of Pro-130 by Gly suggests that the CTT is perpendicular to both the membrane and the main AnaCTDH protein during carotenoid extraction. Finally, the simultaneous mutation of Leu-133, Leu-134 and Leu-136 for alanines showed that the hydrophobicity of the CTT is crucial for carotenoid uptake. Since some substitutions accelerated carotenoid transfer into AnaCTDH while others slowed it down, carotenoprotein properties can be engineered toward the requirements of applications.
Добавил в систему: Егоркин Никита Алексеевич

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Elements of the C-terminal tail of a C-terminal domain homolog of the Orange Carotenoid Protein determining xanthophyll uptake from liposomesстатья

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