Intracellular Localization of Enzymes of Fatty Acid-β-Oxidation in the Alga <i>Cyanidium caldarium</i>

Groß, Wolfgang

doi:10.1104/pp.91.4.1476

Cited by 8 publications

(3 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Most notably, transcripts associated with acyl‐CoA dehydrogenase [EC:1.3.8.7], enoyl‐CoA hydratase [EC:4.2.1.17], and acyl‐CoA oxidase [EC:1.3.3.6] were substantially downregulated during both exponential and stationary growth phases. Given that these enzymes facilitate fatty acid β‐oxidation in mitochondria or in peroxisome (Gross, 1989; Kong et al., 2017), the results suggested their role in decreasing fatty acid turnover rate and in possibly preserving fatty acids under high salinity stress.…”

Section: Resultsmentioning

confidence: 97%

Transcriptomic analysis of Chlorella sp. HS2 suggests the overflow of acetyl‐CoA and NADPH cofactor induces high lipid accumulation and halotolerance

Yun

Pierrelée

Cho

et al. 2020

Food and Energy Security

View full text Add to dashboard Cite

Previously, we isolated Chlorella sp. HS2 (referred hereupon as HS2) from a local tidal rock pool and demonstrated its halotolerance and high biomass productivity under different salinity conditions. To further understand acclimation responses of this alga under high salinity stress, we performed transcriptome analysis of triplicated culture samples grown in freshwater and marine conditions at both exponential and stationary growth phases. The results indicated that the transcripts involved in photosynthesis, TCA, and Calvin cycles were downregulated, whereas the upregulation of DNA repair mechanisms and an ABCB subfamily of eukaryotic type ABC transporter was observed at high salinity condition. In addition, while key enzymes associated with glycolysis pathway and triacylglycerol (TAG) synthesis were determined to be upregulated from early growth phase, salinity stress seemed to reduce the carbohydrate content of harvested biomass from 45.6 dw% to 14.7 dw% and nearly triple the total lipid content from 26.0 dw% to 62.0 dw%. These results suggest that the reallocation of storage carbon toward lipids played a significant role in conferring the viability of this alga under high salinity stress by remediating high level of cellular stress partially resulted from ROS generated in oxygen‐evolving thylakoids as observed in a direct measure of photosystem activities.

show abstract

Section: Resultsmentioning

confidence: 97%

Transcriptomic analysis of Chlorella sp. HS2 suggests the overflow of acetyl‐CoA and NADPH cofactor induces high lipid accumulation and halotolerance

Yun

Pierrelée

Cho

et al. 2020

Food and Energy Security

View full text Add to dashboard Cite

show abstract

“…Dual localization of β-oxidation enzymes was observed in the chlorophyte Eremosphaera and in several Prasinophytes (Winkler et al, 1988 ; Stabenau et al, 1989 ), similar to the situation in mammals. Additionally, solely mitochondrial β-oxidation was observed in the xanthophyte Bumilleriopsis and in Cyanidium (Gross et al, 1985 ; Gross, 1989 ). In C. reinhardtii , an ACOX encoded by CrACX2 was co-localized with peroxisomal CrMDH2 in peroxisomes, indicating at least partial peroxisomal β-oxidation of fatty acids (Kong et al, 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Inferred Subcellular Localization of Peroxisomal Matrix Proteins of Guillardia theta Suggests an Important Role of Peroxisomes in Cryptophytes

Vasilev

Mix²,

Heimerl³

et al. 2022

Front. Plant Sci.

View full text Add to dashboard Cite

Peroxisomes participate in several important metabolic processes in eukaryotic cells, such as the detoxification of reactive oxygen species (ROS) or the degradation of fatty acids by β-oxidation. Recently, the presence of peroxisomes in the cryptophyte Guillardia theta and other “chromalveolates” was revealed by identifying proteins for peroxisomal biogenesis. Here, we investigated the subcellular localization of candidate proteins of G. theta in the diatom Phaeodactylum tricornutum, either possessing a putative peroxisomal targeting signal type 1 (PTS1) sequence or factors lacking a peroxisomal targeting signal but known to be involved in β-oxidation. Our results indicate important contributions of the peroxisomes of G. theta to the carbohydrate, ether phospholipid, nucleotide, vitamin K, ROS, amino acid, and amine metabolisms. Moreover, our results suggest that in contrast to many other organisms, the peroxisomes of G. theta are not involved in the β-oxidation of fatty acids, which exclusively seems to occur in the cryptophyte's mitochondria.

show abstract

“…Although preliminary, the results of this enzymological study fully support the results of previous cell fractionation studies. There is considerable evidence for the occurrence of both mitochondrial and peroxisomal ,3-oxidation in animal, yeast, and some algal (13,36) cells. It is increasingly obvious that, in at least some instances, higher plant cells must be included in this list.…”

Section: Discussionmentioning

confidence: 99%

Partial Purification and Characterization of the Mitochondrial and Peroxisomal Isozymes of Enoyl-Coenzyme A Hydratase from Germinating Pea Seedlings

Miernyk

Thomas²,

Wood³

1991

Plant Physiol.

View full text Add to dashboard Cite

Distinct organellar forms of the j#-oxidation enzyme enoylcoenzyme A (CoA) hydratase were partially purified and characterized from 2-day germinated pea (Pisum sativum L.) seedlings. The purification was accomplished by disruption of purified mitochondria or peroxisomes, (NH4)2SO4 fractionation, and gel permeation chromatography using a column of Sephacryl S-300. The organellar isozymes had distinct kinetic constants for the substrates 2-butenoyl-CoA and 2-octenoyl-CoA, and could be easily distinguished by differences in thermostability and salt activation. The peroxisomal isozyme had a native Mr of 75,000 and appeared to be a typical bifunctional enoyl-CoA hydratase/3-hydroxyacylCoA dehydrogenase, while the mitochondrial isozyme had a native Mr of 57,000 and did not have associated dehydrogenase activity. Western blots of total pea mitochondrial proteins gave a positive signal when probed with anti-rat liver mitochondrial enoyl-CoA hydratase antibodies but there was no signal when blots of total peroxisomal proteins were probed. characteristic of animal cell mitochondrial p-oxidation that distinguishes it from the peroxisomal pathway (18). It has been suggested that the pea mitochondrial ,8-oxidation activity observed by Wood and Thomas could be attributed to peroxisomal contamination (12,20). This criticism ignores the fact that pea mitochondrial f-oxidation requires L-carnitine while the peroxisomal pathway is unable to utilize acylcarnitines (23, 34). Nevertheless, the criticism of peroxisomal contamination was directly addressed and, using an improved purification procedure, it was shown that pea mitochondria devoid of peroxisomal contamination (5) were still fully capable of carnitine-dependent fatty acid f-oxidation (31). Having established the validity of the mitochondrial localization of f-oxidation in peas, it was desirable to compare the physicochemical and catalytic properties of the organelle-specific isozymes. EH3 was chosen for the initial studies because it has the highest in vitro catalytic activity among the f-oxidation enzymes.The subcellular localization of fl-oxidation of fatty acids in plant cells has been a point of some controversy. It was initially assumed that the f-oxidation sequence was localized within mitochondria (14), as was thought to be the case at that time in animal tissues. It was then demonstrated that in the endosperm ofgerminating castor oil seeds the f-oxidation enzymes were colocalized with the enzymes of the glyoxylate cycle within specialized peroxisomes (6). Subsequently, it was demonstrated that fl-oxidation has a dual localization in

show abstract

Intracellular Localization of Enzymes of Fatty Acid-β-Oxidation in the Alga Cyanidium caldarium

Cited by 8 publications

References 32 publications

Transcriptomic analysis of Chlorella sp. HS2 suggests the overflow of acetyl‐CoA and NADPH cofactor induces high lipid accumulation and halotolerance

Transcriptomic analysis of Chlorella sp. HS2 suggests the overflow of acetyl‐CoA and NADPH cofactor induces high lipid accumulation and halotolerance

Inferred Subcellular Localization of Peroxisomal Matrix Proteins of Guillardia theta Suggests an Important Role of Peroxisomes in Cryptophytes

Partial Purification and Characterization of the Mitochondrial and Peroxisomal Isozymes of Enoyl-Coenzyme A Hydratase from Germinating Pea Seedlings

Contact Info

Product

Resources

About