Identification of a cyanobacterial aldehyde dehydrogenase that produces retinoic acid in vitro

Miles, Jennifer A.; Machattou, Petrina; Nevin-Jones, David; Webb, Michael E.; Millard, Andrew; Scanlan, David J.; Taylor, Paul C.

doi:10.1016/j.bbrc.2018.12.171

Cited by 10 publications

(11 citation statements)

References 46 publications

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“…2 has all the hallmarks of the previous definitive analysis of this superfamily from Mei and Dvornyk. However, similar to our previous research on retinoic acid biosynthesis (Miles et al 2019 ; Millard et al 2014 ), we find that inclusion of photolyase/cryptochrome sequences and candidate orthologues from across the kingdoms of life brings to the fore phylogenetic relationships that are particularly relevant to eukaryogenesis, in particular with respect to the placement of animal and bacterial orthologues.…”

Section: Discussionsupporting

confidence: 88%

“…In addition to the large-scale phylogenomic studies that underpin our emerging understanding of eukaryogenesis, the field may benefit from case studies of the evolution of individual genes/proteins across the kingdoms of life. Researchers are finding surprising similarities in chemical signalling-related proteins between animals and groups of complex bacteria, including cyanobacteria (Brash et al 2014 ; Magnani et al 2017 ; Miles et al 2019 ; Millard et al 2014 ; Picciano and Crane 2019 ; Ponting et al 1999 ; Rawlings 2015 ) that pose some important questions about horizontal gene transfer (HGT) in the origin of animals. This offers an alternative perspective from which to view the major transitions in eukaryogenesis.…”

Section: Introductionmentioning

confidence: 99%

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A Case Study of Eukaryogenesis: The Evolution of Photoreception by Photolyase/Cryptochrome Proteins

et al. 2020

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Eukaryogenesis, the origin of the eukaryotes, is still poorly understood. Herein, we show how a detailed all-kingdom phylogenetic analysis overlaid with a map of key biochemical features can provide valuable clues. The photolyase/cryptochrome family of proteins are well known to repair DNA in response to potentially harmful effects of sunlight and to entrain circadian rhythms. Phylogenetic analysis of photolyase/cryptochrome protein sequences from a wide range of prokaryotes and eukaryotes points to a number of horizontal gene transfer events between ancestral bacteria and ancestral eukaryotes. Previous experimental research has characterised patterns of tryptophan residues in these proteins that are important for photoreception, specifically a tryptophan dyad, a canonical tryptophan triad, an alternative tryptophan triad, a tryptophan tetrad and an alternative tetrad. Our results suggest that the spread of the different triad and tetrad motifs across the kingdoms of life accompanied the putative horizontal gene transfers and is consistent with multiple bacterial contributions to eukaryogenesis.

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

A Case Study of Eukaryogenesis: The Evolution of Photoreception by Photolyase/Cryptochrome Proteins

et al. 2020

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“…C. fritschii PCC 6912 is one of only 65 cyanobacterial species to possess orthologs for genes for all three enzymes in the putative retinoic pathway (Miles et al, 2019). These are the UV upregulated gene homolog for carotenoid oxygenase Significant changes in regulation (with log2 fold change > ± 1.3 and p-adj < 0.05) are indicated by magenta shading.…”

Section: Carotenoid Cleavage Enzymesmentioning

confidence: 99%

Synthesis, Regulation and Degradation of Carotenoids Under Low Level UV-B Radiation in the Filamentous Cyanobacterium Chlorogloeopsis fritschii PCC 6912

et al. 2020

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Carotenoids in cyanobacteria play an important role in protecting against and in repairing damage against low level UV-B radiation. Here we use transcriptomics and metabolomic HPLC pigment analysis to compare carotenoid pathway regulation in the filamentous cyanobacterium Chlorogloeopsis fritschii PCC 6912 exposed to white light and to white light supplemented with low level UV-B. Under UV-B changes in carotenoid transcription regulation were found associated with carotenogenesis (carotenoid synthesis), photoprotection and carotenoid cleavage. Transcriptional regulation was reflected in corresponding pigment signatures. All carotenogenesis pathway genes from geranylgeranyl-diphosphate to lycopene were upregulated. There were significant increases in expression of gene homologs (crtW, crtR, cruF, and cruG) associated with routes to ketolation to produce significant increases in echinenone and canthaxanthin concentrations. There were gene homologs for four β-caroteneketolases (crtO and crtW) present but only one crtW was upregulated. Putative genes encoding enzymes (CruF, CrtR, and CruG) for the conversion of γ-carotene to myxol 2 -methylpentoside were upregulated. The hydroxylation pathway to nostaxanthin via zeaxanthin and caloxanthin (gene homologs for CrtR and CrtG) were not upregulated, reflected in the unchanged corresponding pigment concentrations in zeaxanthin, caloxanthin and nostaxanthin, Transcripts for the non-photochemical quenching related Orange-Carotenoid-Protein (OCP) and associated Fluoresence-Recovery-Protein (FRP) associated with photoprotection were upregulated, and one carotenoid binding Helical-Carotenoid-Protein (HCP) gene homolog was downregulated. Multiple copies of genes encoding putative apocarotenoid related carotenoid oxygenases responsible for carotenoid cleavage were identified, including an upregulated apo-β-carotenaloxygenase gene homologous to a retinal producing enzyme. Our study provides holistic insight into the photoregulatory processes that modulate the synthesis, Frontiers in Microbiology | www.frontiersin.org February 2020 | Volume 11 | Article 163 Llewellyn et al. Response of Carotenoids Under Low UV-B in C. fritschiiphotoprotection and cleavage of carotenoids in cyanobacterial cells exposed to low level UV-B. This is important to understanding how regulation of metabolism responds to a changing environment and how metabolism can be modulated for biotechnological purposes.

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“…Recently, characterisation of prokaryotic ALDHs has led to understanding of niche features and characteristics within the superfamily, such as extensions consisting of non-functional domains [ 29 ]. Interestingly, in the last decade, the presence of retinoic acid within prokaryotes was discovered [ 36 , 37 ], highlighting the possibility of retinoid signalling pathways dependent on ALDH and cytochrome oxidases for the conversion of retinaldehyde to retinoic acid. These mechanisms, until recently, were thought to be only of animal origin, but emerging research suggests the contrary [ 36 ].…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, in the last decade, the presence of retinoic acid within prokaryotes was discovered [ 36 , 37 ], highlighting the possibility of retinoid signalling pathways dependent on ALDH and cytochrome oxidases for the conversion of retinaldehyde to retinoic acid. These mechanisms, until recently, were thought to be only of animal origin, but emerging research suggests the contrary [ 36 ].…”

Section: Introductionmentioning

confidence: 99%

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

Shortall

Durack

Magner

et al. 2021

Cells

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Aldehyde dehydrogenases (ALDH), found in all kingdoms of life, form a superfamily of enzymes that primarily catalyse the oxidation of aldehydes to form carboxylic acid products, while utilising the cofactor NAD(P)+. Some superfamily members can also act as esterases using p-nitrophenyl esters as substrates. The ALDHTt from Thermus thermophilus was recombinantly expressed in E. coli and purified to obtain high yields (approximately 15–20 mg/L) and purity utilising an efficient heat treatment step coupled with IMAC and gel filtration chromatography. The use of the heat treatment step proved critical, in its absence decreased yield of 40% was observed. Characterisation of the thermophilic ALDHTt led to optimum enzymatic working conditions of 50 °C, and a pH of 8. ALDHTt possesses dual enzymatic activity, with the ability to act as a dehydrogenase and an esterase. ALDHTt possesses broad substrate specificity, displaying activity for a range of aldehydes, most notably hexanal and the synthetic dialdehyde, terephthalaldehyde. Interestingly, para-substituted benzaldehydes could be processed efficiently, but ortho-substitution resulted in no catalytic activity. Similarly, ALDHTt displayed activity for two different esterase substrates, p-nitrophenyl acetate and p-nitrophenyl butyrate, but with activities of 22.9 and 8.9%, respectively, compared to the activity towards hexanal.

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Identification of a cyanobacterial aldehyde dehydrogenase that produces retinoic acid in vitro

Cited by 10 publications

References 46 publications

A Case Study of Eukaryogenesis: The Evolution of Photoreception by Photolyase/Cryptochrome Proteins

A Case Study of Eukaryogenesis: The Evolution of Photoreception by Photolyase/Cryptochrome Proteins

Synthesis, Regulation and Degradation of Carotenoids Under Low Level UV-B Radiation in the Filamentous Cyanobacterium Chlorogloeopsis fritschii PCC 6912

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

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