The soybean aldehyde dehydrogenase (ALDH) protein superfamily

Kotchoni, Simeon O.; Jiménez-López, José Carlos; Kayodé, A.P.P.; Gachomo, Emma W.; Baba-Moussa, Lamine

doi:10.1016/j.gene.2011.12.035

Cited by 33 publications

(26 citation statements)

References 41 publications

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“…To date, genome-wide analysis of ALDH gene superfamily were performed in many plant species. There were 16 ALDH genes in Arabidopsis [5], 20 in rice [6], 18 in soybean [7], 26 in populus [8], and 23 in maize [9], etc.…”

Section: Introductionmentioning

confidence: 99%

Comparative genomic study of ALDH gene superfamily in Gossypium: A focus on Gossypium hirsutum under salt stress

et al. 2017

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Aldehyde dehydrogenases (ALDHs) are a superfamily of enzymes which play important role in the scavenging of active aldehydes molecules. In present work, a comprehensive whole-genomic study of ALDH gene superfamily was carried out for an allotetraploid cultivated cotton species, G. hirsutum, as well as in parallel relative to their diploid progenitors, G. arboreum and G. raimondii. Totally, 30 and 58 ALDH gene sequences belong to 10 families were identified from diploid and allotetraploid cotton species, respectively. The gene structures among the members from same families were highly conserved. Whole-genome duplication and segmental duplication might be the major driver for the expansion of ALDH gene superfamily in G. hirsutum. In addition, the expression patterns of GhALDH genes were diverse across tissues. Most GhALDH genes were induced or repressed by salt stress in upland cotton. Our observation shed lights on the molecular evolutionary properties of ALDH genes in diploid cottons and their alloallotetraploid derivatives. It may be useful to mine key genes for improvement of cotton response to salt stress.

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Section: Introductionmentioning

confidence: 99%

Comparative genomic study of ALDH gene superfamily in Gossypium: A focus on Gossypium hirsutum under salt stress

et al. 2017

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“…Note that the ALDH families 5, 6, 12, 18, 22 were not found in Glycine max (G.m) [37]. The bar representing G .…”

Section: Resultsmentioning

confidence: 99%

“…Besides the effect of speciation, they appear to evolve through gene duplication as shown in diverse species [31,36,37,39]. Although the driving forces of the duplication events are unclear, it is remarkable that the ALDH genes often do not have the same expression patterns and a number of isoforms per family.…”

Section: Discussionmentioning

confidence: 99%

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Active Sites of Reduced Epidermal Fluorescence1 (REF1) Isoforms Contain Amino Acid Substitutions That Are Different between Monocots and Dicots

2016

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Plant aldehyde dehydrogenases (ALDHs) play important roles in cell wall biosynthesis, growth, development, and tolerance to biotic and abiotic stresses. The Reduced Epidermal Fluorescence1 is encoded by the subfamily 2C of ALDHs and was shown to oxidise coniferaldehyde and sinapaldehyde to ferulic acid and sinapic acid in the phenylpropanoid pathway, respectively. This knowledge has been gained from works in the dicotyledon model species Arabidopsis thaliana then used to functionally annotate ALDH2C isoforms in other species, based on the orthology principle. However, the extent to which the ALDH isoforms differ between monocotyledons and dicotyledons has rarely been accessed side-by-side. In this study, we used a phylogenetic approach to address this question. We have analysed the ALDH genes in Brachypodium distachyon, alongside those of other sequenced monocotyledon and dicotyledon species to examine traits supporting either a convergent or divergent evolution of the ALDH2C/REF1-type proteins. We found that B. distachyon, like other grasses, contains more ALDH2C/REF1 isoforms than A. thaliana and other dicotyledon species. Some amino acid residues in ALDH2C/REF1 isoforms were found as being conserved in dicotyledons but substituted by non-equivalent residues in monocotyledons. One example of those substitutions concerns a conserved phenylalanine and a conserved tyrosine in monocotyledons and dicotyledons, respectively. Protein structure modelling suggests that the presence of tyrosine would widen the substrate-binding pocket in the dicotyledons, and thereby influence substrate specificity. We discussed the importance of these findings as new hints to investigate why ferulic acid contents and cell wall digestibility differ between the dicotyledon and monocotyledon species.

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“…Whatever the reason, it is likely that the ER localization of GFPScFADH observed in this study reflects that of the native protein, because GFP would otherwise locate to the cytosol. It is noteworthy that ScFAO and ScFADH homologs have been identified from other plant species that contain a putative di-Lys ER retention signal, including AtFAO1 (Cheng et al, 2004), LjFAO2 (Zhao et al, 2008), soybean (Glycine max) ALDH3H2 (Kotchoni et al, 2012), and grape ALDH3J1 (Zhang et al, 2012). It would be logical for the fatty alcohol oxidation pathway to be in close proximity to the wax body, since this is also the site of WE hydrolysis (Huang et al, 1978).…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of the Fatty Alcohol Oxidation Pathway for Wax-Ester Mobilization in Germinated Jojoba Seeds

et al. 2012

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Jojoba (Simmondsia chinensis) is the only plant species known to use liquid wax esters (WEs) as a primary seed storage reserve. Upon germination, WE hydrolysis releases very-long-chain fatty alcohols, which must be oxidized to fatty acids by the sequential action of a fatty alcohol oxidase (FAO) and a fatty aldehyde dehydrogenase (FADH) before they can be b-oxidized. Here, we describe the cloning and characterization of genes for each of these two activities. Jojoba FAO and FADH are 52% and 68% identical to Arabidopsis (Arabidopsis thaliana) FAO3 and ALDH3H1, respectively. The genes are expressed most strongly in the cotyledons of jojoba seedlings following germination, but transcripts can also be detected in vegetative tissues. Proteomic analysis indicated that the FAO and FADH proteins can be detected on wax bodies, but they localized to the endoplasmic reticulum when they were expressed as amino-terminal green fluorescent protein fusions in tobacco (Nicotiana tabacum) leaves. Recombinant jojoba FAO and FADH proteins are active on very-long-chain fatty alcohol and fatty aldehyde substrates, respectively, and have biochemical properties consistent with those previously reported in jojoba cotyledons. Coexpression of jojoba FAO and FADH in Arabidopsis enhanced the in vivo rate of fatty alcohol oxidation more than 4-fold. Taken together, our data suggest that jojoba FAO and FADH constitute the very-long-chain fatty alcohol oxidation pathway that is likely to be necessary for efficient WE mobilization following seed germination.

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The soybean aldehyde dehydrogenase (ALDH) protein superfamily

Cited by 33 publications

References 41 publications

Comparative genomic study of ALDH gene superfamily in Gossypium: A focus on Gossypium hirsutum under salt stress

Comparative genomic study of ALDH gene superfamily in Gossypium: A focus on Gossypium hirsutum under salt stress

Active Sites of Reduced Epidermal Fluorescence1 (REF1) Isoforms Contain Amino Acid Substitutions That Are Different between Monocots and Dicots

Molecular Characterization of the Fatty Alcohol Oxidation Pathway for Wax-Ester Mobilization in Germinated Jojoba Seeds

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