A primordial Orange Carotenoid Protein: Structure, photoswitching activity and evolutionary aspects

Slonimskiy, Yury B.; Zupnik, Andrey O.; Varfolomeeva, Larisa A.; Boyko, K.М.; Maksimov, Eugene G.; Sluchanko, Nikolai N.

doi:10.1016/j.ijbiomac.2022.09.131

Cited by 12 publications

(30 citation statements)

References 69 publications

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“…e-g , Predicted aligned errors (PAE). h + i , AlphaFold2 models of OCPx’s CTD from Gloeobacter kilaueensis JS1 do not predict an interaction with SYNY3 FRP at the expected interface (consistent with experimental data 30 ), unless serine (S) at position 264 (SYNY3 numeration) is changed for tyrosine (Y), the ancestral state in AncOCPall that is further shown in overlay here. Inserts show PAEs.…”

Section: Extended Datasupporting

confidence: 75%

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Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection

et al. 2023

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Highly specific interactions between proteins are a fundamental prerequisite for life, but how they evolve remains an unsolved problem. In particular, interactions between initially unrelated proteins require that they evolve matching surfaces. It is unclear whether such surface compatibilities can only be built by selection in small incremental steps, or whether they can also emerge fortuitously. Here, we used molecular phylogenetics, ancestral sequence reconstruction and biophysical characterization of resurrected proteins to retrace the evolution of an allosteric interaction between two proteins that act in the cyanobacterial photoprotection system. We show that this interaction between the orange carotenoid protein (OCP) and its unrelated regulator, the fluorescence recovery protein (FRP), evolved when a precursor of FRP was horizontally acquired by cyanobacteria. FRP’s precursors could already interact with and regulate OCP even before these proteins first encountered each other in an ancestral cyanobacterium. The OCP–FRP interaction exploits an ancient dimer interface in OCP, which also predates the recruitment of FRP into the photoprotection system. Together, our work shows how evolution can fashion complex regulatory systems easily out of pre-existing components.

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Section: Extended Datasupporting

confidence: 75%

“…OCPx paralogues are not affected by FRP any more 16,30 . To identify the underlying structural changes between AncOCPall and OCPx, we repeated the interaction predictions with the CTD of an extant OCPx from Gloeobacter kilaueensis JS1.…”

Section: Ocp and Frpl Drifted In And Out Of Their Ability To Interactmentioning

confidence: 88%

Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection

et al. 2023

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“…Ketocarotenoid production was achieved using E. coli cells carrying the pACCAR25ΔcrtXZcrtO plasmid (chloramphenicol resistance). This plasmid harbors the cluster of the crtY, crtI, crtB, crtE, and crtO genes from Pantoea ananatis, which enables ECH expression 42,56 . Alongside ECH, CAN is also produced in this strain, which may contain various amounts of ECH, CAN, and βCar depending on expression conditions 57,58 .…”

Section: Cloning Protein Expression and Purificationmentioning

confidence: 99%

Insights into the molecular mechanism of yellow cuticle coloration by a chitin-binding carotenoprotein in gregarious locusts

Egorkin,

Dominnik,

Maksimov

et al. 2024

Commun Biol

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Carotenoids are hydrophobic pigments binding to diverse carotenoproteins, many of which remain unexplored. Focusing on yellow gregarious locusts accumulating cuticular carotenoids, here we use engineered Escherichia coli cells to reconstitute a functional water-soluble β-carotene-binding protein, BBP. HPLC and Raman spectroscopy confirmed that recombinant BBP avidly binds β-carotene, inducing the unusual vibronic structure of its absorbance spectrum, just like native BBP extracted from the locust cuticles. Bound to recombinant BBP, β-carotene exhibits pronounced circular dichroism and allows BBP to withstand heating (T0.5 = 68 °C), detergents and pH variations. Using bacteria producing distinct xanthophylls we demonstrate that, while β-carotene is the preferred carotenoid, BBP can also extract from membranes ketocarotenoids and, very poorly, hydroxycarotenoids. We show that BBP-carotenoid complex reversibly binds to chitin, but not to chitosan, implying the role for chitin acetyl groups in cuticular BBP deposition. Reconstructing such locust coloration mechanism in vitro paves the way for structural studies and BBP applications.

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“…The canonical FRP-regulated photoprotection mechanism concerns only the largest OCP1 family, while OCP2 and OCP3 families remain largely underexplored. The heterogeneous OCP3 group apparently combines at least three subfamilies (OCP3a, OCP3b, OCP3c), with OCP3a from Gloeobacteria -the basal cyanobacteria group -being the most primitive and closest to the common OCP ancestor [30]. OCP3 representatives are studied for Scytonema hofmanni PCC 7110 [29], Gloeobacter kilaueensis JS1 [30] and Nostoc flagelliforme [31], with crystal structures for the latter two representatives reported in the last 2 years [30,31].…”

Section: Introductionmentioning

confidence: 99%

Structural framework for the understanding spectroscopic and functional signatures of the cyanobacterial Orange Carotenoid Protein families

Sluchanko,

Maksimov,

Slonimskiy

et al. 2024

International Journal of Biological Macromolecules

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A primordial Orange Carotenoid Protein: Structure, photoswitching activity and evolutionary aspects

Cited by 12 publications

References 69 publications

Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection

Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection

Insights into the molecular mechanism of yellow cuticle coloration by a chitin-binding carotenoprotein in gregarious locusts

Structural framework for the understanding spectroscopic and functional signatures of the cyanobacterial Orange Carotenoid Protein families

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